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Calcium in PDB 1p8j: Crystal Structure of the Proprotein Convertase Furin

Enzymatic activity of Crystal Structure of the Proprotein Convertase Furin

All present enzymatic activity of Crystal Structure of the Proprotein Convertase Furin:
3.4.21.75;

Protein crystallography data

The structure of Crystal Structure of the Proprotein Convertase Furin, PDB code: 1p8j was solved by S.Henrich, A.Cameron, G.P.Bourenkov, R.Kiefersauer, R.Huber, I.Lindberg, W.Bode, M.E.Than, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.82 / 2.60
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 93.305, 135.392, 137.806, 103.56, 98.98, 107.09
R / Rfree (%) 18.8 / 21.9

Calcium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Calcium atom in the Crystal Structure of the Proprotein Convertase Furin (pdb code 1p8j). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 16 binding sites of Calcium where determined in the Crystal Structure of the Proprotein Convertase Furin, PDB code: 1p8j:
Jump to Calcium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Calcium binding site 1 out of 16 in 1p8j

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Calcium binding site 1 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca3001

b:17.2
occ:1.00
O A:VAL205 2.2 19.6 1.0
O A:GLY212 2.3 17.7 1.0
O A:VAL210 2.3 22.6 1.0
OD1 A:ASP115 2.4 23.8 1.0
OD1 A:ASP162 2.4 22.4 1.0
OD1 A:ASN208 2.6 24.3 1.0
OD2 A:ASP162 2.8 22.0 1.0
CG A:ASP162 2.9 21.6 1.0
CG A:ASP115 3.4 23.6 1.0
C A:VAL205 3.4 20.3 1.0
C A:GLY212 3.5 18.6 1.0
C A:VAL210 3.5 23.9 1.0
CG A:ASN208 3.6 24.3 1.0
ND2 A:ASN208 4.0 24.4 1.0
N A:GLY212 4.1 21.5 1.0
CB A:ASP115 4.1 23.8 1.0
N A:VAL210 4.2 25.7 1.0
CA A:VAL210 4.2 24.7 1.0
CA A:GLY212 4.3 18.9 1.0
C A:CYS211 4.3 24.3 1.0
OD2 A:ASP115 4.3 24.7 1.0
N A:ALA206 4.3 21.4 1.0
CA A:ALA206 4.3 21.8 1.0
CB A:VAL210 4.4 25.3 1.0
CA A:VAL205 4.4 19.9 1.0
CB A:ASP162 4.4 21.5 1.0
N A:VAL213 4.5 17.9 1.0
N A:VAL205 4.5 19.0 1.0
N A:CYS211 4.5 24.5 1.0
CG1 A:VAL213 4.6 19.0 1.0
CA A:VAL213 4.6 18.2 1.0
O A:CYS211 4.6 25.4 1.0
O A:HOH4114 4.7 14.7 1.0
CB A:VAL205 4.7 20.4 1.0
N A:ASN208 4.8 23.0 1.0
CA A:CYS211 4.8 25.9 1.0
C A:ALA206 4.8 22.1 1.0
CB A:CYS211 4.9 28.1 1.0
C A:ALA204 4.9 19.1 1.0
CB A:ASN208 4.9 23.4 1.0
N A:ASN207 4.9 22.4 1.0

Calcium binding site 2 out of 16 in 1p8j

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Calcium binding site 2 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca3002

b:7.6
occ:1.00
OD1 A:ASP258 2.2 13.0 1.0
OE1 A:GLU331 2.3 15.6 1.0
O A:HOH4270 2.3 5.2 1.0
O A:HOH4271 2.3 3.5 1.0
OD1 A:ASP301 2.4 14.4 1.0
O A:HOH4269 2.4 8.9 1.0
OE2 A:GLU331 2.5 15.1 1.0
CD A:GLU331 2.7 15.2 1.0
CG A:ASP301 3.3 17.0 1.0
CG A:ASP258 3.3 14.6 1.0
NH1 J:AR7805 3.9 15.4 1.0
OD2 A:ASP301 4.0 18.1 1.0
CB A:ASP258 4.0 14.9 1.0
CB A:ASP301 4.1 16.1 1.0
CA A:ASP258 4.1 15.2 1.0
CG A:GLU331 4.2 13.8 1.0
OD2 A:ASP258 4.2 13.5 1.0
O A:HOH4138 4.2 10.0 1.0
CA A:GLY294 4.4 14.6 1.0
O A:SER293 4.4 15.2 1.0
O A:HOH4081 4.5 15.6 1.0
O A:SER302 4.6 20.8 1.0
OD2 A:ASP306 4.6 10.0 1.0
CZ J:AR7805 4.6 15.1 1.0
O A:GLU257 4.7 12.7 1.0
CB A:ASP306 4.7 12.1 1.0
CA A:CYS303 4.8 20.4 1.0
N A:GLY296 4.8 17.5 1.0
O A:PRO256 4.9 14.4 1.0
C A:SER302 4.9 19.6 1.0
N A:ASP258 5.0 14.8 1.0
N A:CYS303 5.0 19.2 1.0

Calcium binding site 3 out of 16 in 1p8j

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Calcium binding site 3 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca3003

b:18.4
occ:1.00
O B:VAL205 2.2 22.4 1.0
O B:VAL210 2.3 25.6 1.0
OD1 B:ASP162 2.4 24.2 1.0
O B:GLY212 2.4 20.6 1.0
OD1 B:ASP115 2.4 26.4 1.0
OD1 B:ASN208 2.5 25.9 1.0
OD2 B:ASP162 2.8 21.5 1.0
CG B:ASP162 2.9 21.5 1.0
C B:VAL205 3.4 22.3 1.0
CG B:ASN208 3.4 25.8 1.0
CG B:ASP115 3.4 26.2 1.0
C B:VAL210 3.5 26.2 1.0
C B:GLY212 3.6 21.7 1.0
ND2 B:ASN208 3.8 26.6 1.0
CB B:ASP115 4.1 25.5 1.0
N B:VAL210 4.1 26.8 1.0
N B:GLY212 4.1 24.2 1.0
CA B:VAL210 4.2 25.6 1.0
C B:CYS211 4.3 25.6 1.0
CB B:VAL210 4.3 25.6 1.0
N B:ALA206 4.3 22.4 1.0
CA B:ALA206 4.4 22.6 1.0
CA B:GLY212 4.4 22.5 1.0
OD2 B:ASP115 4.4 24.8 1.0
CA B:VAL205 4.4 22.4 1.0
CB B:ASP162 4.4 20.9 1.0
N B:VAL205 4.5 21.7 1.0
N B:CYS211 4.5 26.7 1.0
N B:VAL213 4.6 20.4 1.0
O B:CYS211 4.6 26.1 1.0
CG1 B:VAL213 4.6 20.3 1.0
N B:ASN208 4.7 24.9 1.0
CB B:VAL205 4.7 22.3 1.0
CA B:VAL213 4.7 20.4 1.0
CB B:ASN208 4.7 24.4 1.0
C B:ALA206 4.8 23.2 1.0
CA B:CYS211 4.8 26.3 1.0
CB B:CYS211 4.9 28.0 1.0
N B:ASN207 4.9 23.2 1.0
C B:ALA204 4.9 21.7 1.0
CG1 B:VAL210 4.9 25.2 1.0

Calcium binding site 4 out of 16 in 1p8j

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Calcium binding site 4 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca3004

b:11.2
occ:1.00
OD1 B:ASP258 2.2 12.3 1.0
O B:HOH4199 2.2 1.9 1.0
OE1 B:GLU331 2.3 12.5 1.0
OD1 B:ASP301 2.4 14.9 1.0
O B:HOH4248 2.4 4.5 1.0
O B:HOH4258 2.4 9.3 1.0
OE2 B:GLU331 2.4 10.5 1.0
CD B:GLU331 2.6 12.4 1.0
CG B:ASP301 3.3 14.3 1.0
CG B:ASP258 3.3 17.0 1.0
OD2 B:ASP301 4.0 14.6 1.0
CB B:ASP258 4.0 16.5 1.0
CB B:ASP301 4.1 16.5 1.0
NH1 K:AR7805 4.1 11.5 1.0
CA B:ASP258 4.1 16.9 1.0
CG B:GLU331 4.1 12.6 1.0
OD2 B:ASP258 4.2 16.9 1.0
CA B:GLY294 4.4 15.3 1.0
O B:SER293 4.4 16.1 1.0
O B:SER302 4.5 20.2 1.0
O B:HOH4200 4.6 12.2 1.0
O B:HOH4074 4.6 9.8 1.0
OD2 B:ASP306 4.7 8.2 1.0
O B:GLU257 4.7 14.4 1.0
CA B:CYS303 4.7 19.2 1.0
CB B:ASP306 4.8 11.1 1.0
CZ K:AR7805 4.8 13.1 1.0
N B:GLY296 4.8 17.0 1.0
C B:SER302 4.8 20.1 1.0
O B:PRO256 5.0 12.4 1.0
N B:CYS303 5.0 20.1 1.0
N B:ASP258 5.0 16.0 1.0
CB B:GLU331 5.0 14.4 1.0

Calcium binding site 5 out of 16 in 1p8j

Go back to Calcium Binding Sites List in 1p8j
Calcium binding site 5 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 5 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca3005

b:21.5
occ:1.00
O C:VAL210 2.2 22.2 1.0
O C:VAL205 2.3 18.4 1.0
O C:GLY212 2.3 19.7 1.0
OD1 C:ASP115 2.4 25.8 1.0
OD1 C:ASP162 2.4 20.6 1.0
OD1 C:ASN208 2.5 24.7 1.0
OD2 C:ASP162 2.7 22.8 1.0
CG C:ASP162 2.9 21.5 1.0
C C:VAL210 3.4 23.4 1.0
CG C:ASP115 3.4 24.5 1.0
C C:VAL205 3.5 20.2 1.0
C C:GLY212 3.5 19.1 1.0
CG C:ASN208 3.5 23.4 1.0
ND2 C:ASN208 3.9 23.5 1.0
N C:GLY212 4.1 21.6 1.0
CB C:ASP115 4.1 23.9 1.0
N C:VAL210 4.1 23.8 1.0
CA C:VAL210 4.1 22.6 1.0
C C:CYS211 4.3 24.2 1.0
CB C:VAL210 4.3 22.8 1.0
CA C:GLY212 4.3 18.9 1.0
N C:ALA206 4.4 20.9 1.0
OD2 C:ASP115 4.4 23.0 1.0
CB C:ASP162 4.4 20.6 1.0
CA C:ALA206 4.4 22.0 1.0
CA C:VAL205 4.5 19.6 1.0
N C:CYS211 4.5 23.4 1.0
N C:VAL205 4.5 19.4 1.0
N C:VAL213 4.5 18.4 1.0
O C:HOH4116 4.6 12.8 1.0
CG1 C:VAL213 4.6 17.7 1.0
O C:CYS211 4.6 24.9 1.0
CA C:VAL213 4.7 18.2 1.0
CA C:CYS211 4.7 24.8 1.0
N C:ASN208 4.8 23.3 1.0
CB C:CYS211 4.8 27.3 1.0
CB C:VAL205 4.8 19.0 1.0
C C:ALA206 4.8 21.9 1.0
CB C:ASN208 4.9 22.8 1.0
C C:ALA204 4.9 18.6 1.0
N C:ASN207 4.9 23.1 1.0
CG1 C:VAL210 4.9 20.9 1.0

Calcium binding site 6 out of 16 in 1p8j

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Calcium binding site 6 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 6 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca3006

b:10.1
occ:1.00
O C:HOH4135 2.2 6.7 1.0
OE1 C:GLU331 2.3 15.4 1.0
OD1 C:ASP258 2.3 14.9 1.0
OD1 C:ASP301 2.4 15.6 1.0
O C:HOH4102 2.4 11.6 1.0
O C:HOH4063 2.4 0.8 1.0
OE2 C:GLU331 2.5 12.4 1.0
CD C:GLU331 2.7 14.5 1.0
CG C:ASP301 3.3 17.6 1.0
CG C:ASP258 3.4 15.8 1.0
OD2 C:ASP301 4.0 20.4 1.0
CB C:ASP258 4.0 15.1 1.0
NH1 L:AR7805 4.1 15.4 1.0
CB C:ASP301 4.1 17.4 1.0
CA C:ASP258 4.2 15.4 1.0
CG C:GLU331 4.2 13.0 1.0
OD2 C:ASP258 4.3 14.7 1.0
O C:SER293 4.4 17.4 1.0
CA C:GLY294 4.4 14.2 1.0
O C:HOH4263 4.4 16.4 1.0
O C:HOH4134 4.5 7.5 1.0
O C:SER302 4.5 20.6 1.0
OD2 C:ASP306 4.6 9.3 1.0
O C:GLU257 4.6 13.2 1.0
CB C:ASP306 4.7 11.7 1.0
CA C:CYS303 4.7 20.7 1.0
CZ L:AR7805 4.7 14.2 1.0
C C:SER302 4.8 20.1 1.0
N C:GLY296 4.8 15.4 1.0
O C:PRO256 4.9 14.2 1.0
N C:CYS303 4.9 20.2 1.0

Calcium binding site 7 out of 16 in 1p8j

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Calcium binding site 7 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 7 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ca3007

b:29.7
occ:1.00
O D:VAL205 2.2 22.8 1.0
O D:VAL210 2.3 27.0 1.0
O D:GLY212 2.3 26.2 1.0
OD1 D:ASP162 2.3 28.2 1.0
OD1 D:ASP115 2.4 30.2 1.0
OD1 D:ASN208 2.6 28.4 1.0
OD2 D:ASP162 2.7 28.7 1.0
CG D:ASP162 2.9 27.3 1.0
C D:VAL205 3.4 24.3 1.0
CG D:ASP115 3.4 29.5 1.0
C D:VAL210 3.5 28.0 1.0
C D:GLY212 3.5 24.5 1.0
CG D:ASN208 3.5 28.8 1.0
ND2 D:ASN208 3.9 28.7 1.0
N D:GLY212 4.1 26.5 1.0
CB D:ASP115 4.1 28.5 1.0
N D:VAL210 4.2 28.3 1.0
CA D:VAL210 4.2 28.0 1.0
N D:ALA206 4.3 25.2 1.0
CA D:ALA206 4.3 25.5 1.0
C D:CYS211 4.3 27.6 1.0
CA D:GLY212 4.3 24.6 1.0
CB D:VAL210 4.3 28.2 1.0
OD2 D:ASP115 4.3 29.4 1.0
CA D:VAL205 4.3 23.8 1.0
CB D:ASP162 4.4 25.9 1.0
N D:VAL205 4.4 23.5 1.0
CG1 D:VAL213 4.5 22.4 1.0
N D:VAL213 4.5 23.3 1.0
N D:CYS211 4.5 28.6 1.0
O D:CYS211 4.6 27.8 1.0
CA D:VAL213 4.6 22.5 1.0
CB D:VAL205 4.7 23.0 1.0
C D:ALA206 4.8 25.7 1.0
N D:ASN208 4.8 26.5 1.0
CA D:CYS211 4.8 28.9 1.0
CB D:ASN208 4.8 27.8 1.0
C D:ALA204 4.8 23.4 1.0
CB D:CYS211 4.8 31.6 1.0
CG1 D:VAL210 4.9 25.9 1.0
N D:ASN207 4.9 26.5 1.0

Calcium binding site 8 out of 16 in 1p8j

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Calcium binding site 8 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 8 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ca3008

b:16.6
occ:1.00
O D:HOH4160 2.3 13.3 1.0
OD1 D:ASP258 2.3 20.0 1.0
OE1 D:GLU331 2.3 15.6 1.0
O D:HOH4192 2.3 12.8 1.0
OD1 D:ASP301 2.3 19.4 1.0
O D:HOH4070 2.4 10.8 1.0
OE2 D:GLU331 2.4 13.8 1.0
CD D:GLU331 2.7 15.4 1.0
CG D:ASP301 3.2 18.3 1.0
CG D:ASP258 3.4 19.9 1.0
OD2 D:ASP301 3.9 18.3 1.0
CB D:ASP258 4.1 18.6 1.0
CB D:ASP301 4.1 19.1 1.0
CA D:ASP258 4.1 18.7 1.0
NH1 M:AR7805 4.2 16.1 1.0
CG D:GLU331 4.2 15.5 1.0
OD2 D:ASP258 4.4 19.8 1.0
O D:SER302 4.4 20.3 1.0
O D:SER293 4.5 18.9 1.0
CA D:GLY294 4.5 17.6 1.0
O D:GLU257 4.7 16.8 1.0
OD2 D:ASP306 4.7 15.6 1.0
CB D:ASP306 4.7 14.6 1.0
CA D:CYS303 4.7 21.0 1.0
C D:SER302 4.8 20.7 1.0
CZ M:AR7805 4.8 16.7 1.0
O D:PRO256 4.9 17.9 1.0
N D:GLY296 4.9 18.8 1.0
N D:CYS303 4.9 21.4 1.0
N D:ASP258 5.0 18.4 1.0

Calcium binding site 9 out of 16 in 1p8j

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Calcium binding site 9 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 9 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca3009

b:22.0
occ:1.00
O E:VAL205 2.2 20.6 1.0
O E:GLY212 2.3 17.8 1.0
O E:VAL210 2.3 21.7 1.0
OD1 E:ASP162 2.4 25.8 1.0
OD1 E:ASP115 2.4 28.1 1.0
OD1 E:ASN208 2.6 28.3 1.0
OD2 E:ASP162 2.8 24.8 1.0
CG E:ASP162 2.9 24.4 1.0
CG E:ASP115 3.4 26.1 1.0
C E:VAL205 3.4 21.3 1.0
C E:GLY212 3.5 18.9 1.0
C E:VAL210 3.5 23.1 1.0
CG E:ASN208 3.6 26.8 1.0
ND2 E:ASN208 4.0 28.0 1.0
N E:GLY212 4.1 21.8 1.0
CB E:ASP115 4.1 24.9 1.0
N E:VAL210 4.2 24.2 1.0
CA E:VAL210 4.2 23.6 1.0
CA E:GLY212 4.3 19.0 1.0
N E:ALA206 4.3 22.4 1.0
CA E:ALA206 4.3 23.3 1.0
OD2 E:ASP115 4.3 26.3 1.0
C E:CYS211 4.3 24.1 1.0
CB E:VAL210 4.4 23.2 1.0
CA E:VAL205 4.4 20.8 1.0
CB E:ASP162 4.4 22.6 1.0
N E:VAL213 4.5 18.5 1.0
N E:VAL205 4.5 21.0 1.0
CG1 E:VAL213 4.5 18.8 1.0
O E:HOH4147 4.5 11.4 1.0
N E:CYS211 4.6 23.3 1.0
CA E:VAL213 4.6 18.7 1.0
O E:CYS211 4.7 23.5 1.0
CB E:VAL205 4.7 20.9 1.0
C E:ALA206 4.8 24.1 1.0
N E:ASN208 4.8 24.8 1.0
CA E:CYS211 4.8 25.0 1.0
C E:ALA204 4.9 20.5 1.0
CB E:CYS211 4.9 27.5 1.0
N E:ASN207 4.9 24.4 1.0
CB E:ASN208 4.9 24.8 1.0
CB E:ALA204 5.0 16.8 1.0

Calcium binding site 10 out of 16 in 1p8j

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Calcium binding site 10 out of 16 in the Crystal Structure of the Proprotein Convertase Furin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 10 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca3010

b:9.8
occ:1.00
OD1 E:ASP258 2.2 16.5 1.0
OE1 E:GLU331 2.2 13.1 1.0
O E:HOH4104 2.3 4.7 1.0
O E:HOH4253 2.3 5.1 1.0
O E:HOH4252 2.3 7.8 1.0
OD1 E:ASP301 2.4 17.0 1.0
OE2 E:GLU331 2.5 10.9 1.0
CD E:GLU331 2.7 13.3 1.0
CG E:ASP258 3.3 16.9 1.0
CG E:ASP301 3.3 18.5 1.0
NH1 N:AR7805 3.9 9.1 1.0
CB E:ASP258 4.1 15.4 1.0
OD2 E:ASP301 4.1 18.7 1.0
OD2 E:ASP258 4.2 15.3 1.0
CA E:ASP258 4.2 15.4 1.0
CB E:ASP301 4.2 18.3 1.0
CG E:GLU331 4.2 12.1 1.0
O E:SER293 4.3 15.8 1.0
CA E:GLY294 4.3 12.9 1.0
O E:HOH4083 4.5 5.9 1.0
OD2 E:ASP306 4.5 13.2 1.0
O E:SER302 4.5 20.7 1.0
CZ N:AR7805 4.6 10.3 1.0
CB E:ASP306 4.7 13.0 1.0
O E:GLU257 4.7 13.8 1.0
CA E:CYS303 4.7 19.3 1.0
O E:PRO256 4.8 14.9 1.0
N E:GLY296 4.9 17.1 1.0
C E:SER302 4.9 18.9 1.0
N E:CYS303 5.0 18.3 1.0
C E:GLY294 5.0 14.6 1.0

Reference:

S.Henrich, A.Cameron, G.P.Bourenkov, R.Kiefersauer, R.Huber, I.Lindberg, W.Bode, M.E.Than. The Crystal Structure of the Proprotein Processing Proteinase Furin Explains Its Stringent Specificity Nat.Struct.Biol. V. 10 520 2003.
ISSN: ISSN 1072-8368
PubMed: 12794637
DOI: 10.1038/NSB941
Page generated: Thu Jul 11 13:40:16 2024

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