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Chlorine in PDB 4c2r: Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q

Enzymatic activity of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q

All present enzymatic activity of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q, PDB code: 4c2r 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) 28.83 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.450, 84.804, 134.023, 90.00, 90.00, 90.00
R / Rfree (%) 20.126 / 23.783

Other elements in 4c2r:

The structure of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q (pdb code 4c2r). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q, PDB code: 4c2r:

Chlorine binding site 1 out of 1 in 4c2r

Go back to Chlorine Binding Sites List in 4c2r
Chlorine binding site 1 out of 1 in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522Q within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl702

b:28.7
occ:1.00
 O A:HOH2039 3.1 34.4 1.0
NE A:ARG186 3.3 21.0 1.0
NH2 A:ARG186 3.3 20.0 1.0
NE1 A:TRP485 3.4 21.7 1.0
NH2 A:ARG489 3.5 20.2 1.0
CZ2 A:TRP486 3.6 20.8 1.0
CZ A:ARG186 3.7 20.6 1.0
CB A:ASP507 3.8 20.6 1.0
NE A:ARG489 3.9 20.1 1.0
CZ A:ARG489 3.9 19.9 1.0
CH2 A:TRP486 3.9 20.8 1.0
CE2 A:TRP485 4.2 21.6 1.0
CD1 A:TRP485 4.3 22.0 1.0
CD A:ARG186 4.4 21.6 1.0
CE2 A:TRP486 4.4 20.7 1.0
CZ2 A:TRP182 4.4 20.6 1.0
CZ2 A:TRP485 4.4 21.6 1.0
O A:ASP507 4.5 20.1 1.0
CG A:ASP507 4.7 20.8 1.0
C A:ASP507 4.7 20.1 1.0
O A:HOH2036 4.7 22.1 1.0
CA A:ASP507 4.9 20.6 1.0
NE1 A:TRP486 4.9 20.8 1.0
NH1 A:ARG489 4.9 19.5 1.0
OD2 A:ASP507 4.9 21.3 1.0
CD A:ARG489 5.0 20.1 1.0
CZ3 A:TRP486 5.0 20.8 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: Fri Jul 11 13:42:59 2025

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