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Zinc in PDB 4c2p: Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril

Enzymatic activity of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril

All present enzymatic activity of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril, PDB code: 4c2p was solved by G.Masuyer, C.J.Yates, S.L.U.Schwager, A.Mohd, E.D.Sturrock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.74 / 1.99
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.140, 84.650, 135.180, 90.00, 90.00, 90.00
R / Rfree (%) 21.124 / 24.67

Other elements in 4c2p:

The structure of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril (pdb code 4c2p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril, PDB code: 4c2p:

Zinc binding site 1 out of 1 in 4c2p

Go back to Zinc Binding Sites List in 4c2p
Zinc binding site 1 out of 1 in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:26.5
occ:1.00
 OE1 A:GLU411 2.0 14.1 1.0
NE2 A:HIS387 2.1 17.6 1.0
NE2 A:HIS383 2.2 22.5 1.0
S A:X8Z709 2.4 32.4 1.0
CD A:GLU411 2.9 14.0 1.0
CE1 A:HIS387 2.9 17.5 1.0
CE1 A:HIS383 3.0 22.4 1.0
CD2 A:HIS383 3.1 22.8 1.0
OE2 A:GLU411 3.1 14.1 1.0
CD2 A:HIS387 3.2 17.8 1.0
C1 A:X8Z709 3.7 30.8 1.0
C2 A:X8Z709 4.0 30.1 1.0
ND1 A:HIS387 4.1 17.6 1.0
ND1 A:HIS383 4.1 22.4 1.0
CG A:HIS383 4.1 22.8 1.0
O A:HOH1335 4.2 33.6 1.0
CG A:GLU411 4.2 13.7 1.0
CG A:HIS387 4.3 17.9 1.0
OE2 A:GLU384 4.4 21.1 1.0
CE1 A:TYR523 4.5 11.4 1.0
CA A:GLU411 4.5 13.7 1.0
CB A:GLU411 4.6 13.5 1.0
OE1 A:GLU384 4.8 21.5 1.0
CD A:GLU384 4.9 21.3 1.0
OH A:TYR523 4.9 12.0 1.0
C3 A:X8Z709 5.0 30.6 1.0
C4 A:X8Z709 5.0 29.4 1.0

Reference:

C.J.Yates, G.Masuyer, S.L.U.Schwager, A.Mohd, E.D.Sturrock, K.R.Acharya. Molecular and Thermodynamic Mechanisms of the Chloride Dependent Human Angiotensin-I Converting Enzyme (Ace) J.Biol.Chem. V. 289 1798 2014.
ISSN: ISSN 0021-9258
PubMed: 24297181
DOI: 10.1074/JBC.M113.512335
Page generated: Wed Dec 16 05:07:20 2020

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