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Calcium in PDB 5jxj: Structure of the Proprotein Convertase Furin Complexed to Meta- Guanidinomethyl-Phac-Rvr-Amba in Presence of Edta

Enzymatic activity of Structure of the Proprotein Convertase Furin Complexed to Meta- Guanidinomethyl-Phac-Rvr-Amba in Presence of Edta

All present enzymatic activity of Structure of the Proprotein Convertase Furin Complexed to Meta- Guanidinomethyl-Phac-Rvr-Amba in Presence of Edta:
3.4.21.75;

Protein crystallography data

The structure of Structure of the Proprotein Convertase Furin Complexed to Meta- Guanidinomethyl-Phac-Rvr-Amba in Presence of Edta, PDB code: 5jxj 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) 43.23 / 2.00
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 132.080, 132.080, 155.642, 90.00, 90.00, 120.00
R / Rfree (%) 16.7 / 18.9

Other elements in 5jxj:

The structure of Structure of the Proprotein Convertase Furin Complexed to Meta- Guanidinomethyl-Phac-Rvr-Amba in Presence of Edta also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 6 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of the Proprotein Convertase Furin Complexed to Meta- Guanidinomethyl-Phac-Rvr-Amba in Presence of Edta (pdb code 5jxj). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of the Proprotein Convertase Furin Complexed to Meta- Guanidinomethyl-Phac-Rvr-Amba in Presence of Edta, PDB code: 5jxj:

Calcium binding site 1 out of 1 in 5jxj

Go back to Calcium Binding Sites List in 5jxj
Calcium binding site 1 out of 1 in the Structure of the Proprotein Convertase Furin Complexed to Meta- Guanidinomethyl-Phac-Rvr-Amba in Presence of Edta


Mono view


Stereo pair view

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

b:24.9
occ:1.00
 O A:VAL210 2.3 22.3 1.0
O A:VAL205 2.3 25.7 1.0
O A:GLY212 2.4 22.6 1.0
OD2 A:ASP115 2.4 24.4 1.0
OD1 A:ASP162 2.5 25.6 1.0
OD2 A:ASP162 2.5 26.4 1.0
OD1 A:ASN208 2.6 25.9 1.0
CG A:ASP162 2.9 29.5 1.0
CG A:ASP115 3.5 21.4 1.0
C A:VAL205 3.5 24.7 1.0
C A:VAL210 3.5 29.5 1.0
CG A:ASN208 3.6 29.2 1.0
C A:GLY212 3.6 30.1 1.0
ND2 A:ASN208 3.9 19.0 1.0
CB A:ASP115 4.1 21.8 1.0
N A:GLY212 4.1 22.7 1.0
CA A:VAL210 4.3 20.8 1.0
N A:VAL210 4.3 28.8 1.0
C A:CYS211 4.3 28.3 1.0
CA A:ALA206 4.4 25.4 1.0
CA A:GLY212 4.4 19.3 1.0
N A:ALA206 4.4 23.1 1.0
CB A:ASP162 4.4 22.9 1.0
CB A:VAL210 4.4 25.5 1.0
OD1 A:ASP115 4.4 24.7 1.0
CA A:VAL205 4.5 23.2 1.0
N A:VAL205 4.5 21.1 1.0
N A:CYS211 4.5 23.4 1.0
N A:VAL213 4.6 23.8 1.0
O A:HOH894 4.7 23.6 1.0
O A:CYS211 4.7 23.6 1.0
CG1 A:VAL213 4.7 27.0 1.0
CA A:VAL213 4.7 22.6 1.0
C A:ALA206 4.7 26.6 1.0
CA A:CYS211 4.8 25.1 1.0
N A:ASN208 4.8 27.0 1.0
CB A:VAL205 4.8 28.4 1.0
CB A:CYS211 4.8 24.6 1.0
N A:ASN207 4.8 28.3 1.0
C A:ALA204 4.9 20.9 1.0
CB A:ASN208 4.9 28.9 1.0
CG1 A:VAL210 4.9 30.4 1.0
CB A:ALA204 5.0 17.4 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: Mon Jul 15 06:37:46 2024

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