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Calcium in PDB 5jxh: Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.

Enzymatic activity of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.

All present enzymatic activity of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.:
3.4.21.75;

Protein crystallography data

The structure of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution., PDB code: 5jxh was solved by S.O.Dahms, M.Arciniega, T.Steinmetzer, R.Huber, M.E.Than, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.14 / 2.00
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 131.790, 131.790, 155.578, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / 18.5

Other elements in 5jxh:

The structure of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution. also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution. (pdb code 5jxh). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution., PDB code: 5jxh:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 5jxh

Go back to Calcium Binding Sites List in 5jxh
Calcium binding site 1 out of 3 in the Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca601

b:25.8
occ:1.00
 O A:ASP181 2.3 23.1 1.0
OD2 A:ASP174 2.3 22.6 1.0
O A:HOH859 2.5 22.9 1.0
OD1 A:ASP179 2.5 25.7 1.0
O A:HOH780 2.5 25.0 1.0
O A:HOH1131 2.5 27.4 1.0
OD2 A:ASP179 2.6 30.1 1.0
CG A:ASP179 2.9 26.9 1.0
CG A:ASP174 3.3 24.3 1.0
C A:ASP181 3.5 19.9 1.0
CB A:ASP174 3.6 21.5 1.0
CB A:ASP181 4.0 23.3 1.0
CA A:ASP181 4.1 18.8 1.0
N A:ASP181 4.3 23.4 1.0
CB A:ASP179 4.4 22.4 1.0
OD1 A:ASP174 4.5 19.8 1.0
NH2 A:ARG225 4.5 24.7 1.0
N A:PRO182 4.5 21.0 1.0
CG A:ASP181 4.5 36.2 1.0
CB A:ASP177 4.6 25.1 1.0
OD2 A:ASP177 4.6 34.7 1.0
O A:GLN183 4.8 18.7 1.0
N A:GLN183 4.8 21.8 1.0
CA A:PRO182 4.8 21.7 1.0
OD1 A:ASP181 4.9 27.9 1.0
O A:HOH1169 4.9 40.6 1.0

Calcium binding site 2 out of 3 in 5jxh

Go back to Calcium Binding Sites List in 5jxh
Calcium binding site 2 out of 3 in the Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca602

b:24.2
occ:1.00
 O A:VAL210 2.3 22.7 1.0
O A:VAL205 2.3 21.5 1.0
O A:GLY212 2.4 23.2 1.0
OD2 A:ASP115 2.4 22.4 1.0
OD1 A:ASP162 2.4 24.1 1.0
OD2 A:ASP162 2.5 23.5 1.0
OD1 A:ASN208 2.6 25.7 1.0
CG A:ASP162 2.8 26.1 1.0
C A:VAL210 3.5 27.1 1.0
CG A:ASP115 3.5 22.0 1.0
C A:VAL205 3.5 22.2 1.0
CG A:ASN208 3.6 26.6 1.0
C A:GLY212 3.6 27.8 1.0
ND2 A:ASN208 3.9 21.1 1.0
CB A:ASP115 4.1 23.1 1.0
N A:GLY212 4.1 24.7 1.0
CA A:VAL210 4.2 25.6 1.0
N A:VAL210 4.3 24.0 1.0
C A:CYS211 4.3 28.5 1.0
CB A:ASP162 4.3 20.6 1.0
CB A:VAL210 4.3 25.2 1.0
CA A:GLY212 4.4 19.0 1.0
CA A:ALA206 4.4 20.6 1.0
N A:ALA206 4.4 23.5 1.0
OD1 A:ASP115 4.4 22.7 1.0
CA A:VAL205 4.5 20.2 1.0
N A:VAL205 4.5 24.1 1.0
N A:CYS211 4.5 25.1 1.0
N A:VAL213 4.6 20.7 1.0
O A:CYS211 4.6 23.6 1.0
CA A:VAL213 4.7 17.4 1.0
CG1 A:VAL213 4.7 22.4 1.0
O A:HOH958 4.7 21.7 1.0
CA A:CYS211 4.8 22.1 1.0
C A:ALA206 4.8 24.3 1.0
CB A:CYS211 4.8 28.9 1.0
CB A:VAL205 4.8 26.4 1.0
N A:ASN208 4.8 26.1 1.0
CG1 A:VAL210 4.9 29.5 1.0
CB A:ASN208 4.9 31.1 1.0
N A:ASN207 4.9 26.1 1.0
C A:ALA204 4.9 20.8 1.0

Calcium binding site 3 out of 3 in 5jxh

Go back to Calcium Binding Sites List in 5jxh
Calcium binding site 3 out of 3 in the Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca603

b:15.0
occ:1.00
 OD2 A:ASP301 2.4 15.3 1.0
OE1 A:GLU331 2.4 17.3 1.0
O A:HOH815 2.4 13.0 1.0
OD1 A:ASP258 2.4 17.5 1.0
O A:HOH973 2.4 15.9 1.0
OE2 A:GLU331 2.4 16.7 1.0
O A:HOH856 2.5 14.3 1.0
CD A:GLU331 2.8 17.2 1.0
CG A:ASP301 3.3 16.9 1.0
CG A:ASP258 3.5 19.6 1.0
OD1 A:ASP301 4.0 15.7 1.0
CB A:ASP301 4.1 16.5 1.0
N35 H:00S5 4.2 13.7 1.0
CB A:ASP258 4.2 17.3 1.0
CA A:ASP258 4.2 17.4 1.0
CG A:GLU331 4.3 14.6 1.0
O A:HOH924 4.3 19.5 1.0
OD2 A:ASP258 4.4 17.2 1.0
O A:SER302 4.5 16.0 1.0
O A:SER293 4.5 15.4 1.0
OD2 A:ASP306 4.5 16.3 1.0
O A:HOH942 4.5 16.9 1.0
CA A:GLY294 4.6 14.4 1.0
O A:GLU257 4.7 16.0 1.0
CB A:ASP306 4.7 14.3 1.0
CA A:CYS303 4.8 15.4 1.0
C27 H:00S5 4.8 17.2 1.0
C A:SER302 4.8 18.7 1.0
N A:GLY296 4.9 16.5 1.0
O A:PRO256 4.9 17.8 1.0
N A:ASP258 5.0 16.6 1.0

Reference:

S.O.Dahms, M.Arciniega, T.Steinmetzer, R.Huber, M.E.Than. Structure of the Unliganded Form of the Proprotein Convertase Furin Suggests Activation By A Substrate-Induced Mechanism. Proc.Natl.Acad.Sci.Usa V. 113 11196 2016.
ISSN: ESSN 1091-6490
PubMed: 27647913
DOI: 10.1073/PNAS.1613630113
Page generated: Wed Jul 9 07:14:37 2025

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