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Zinc in PDB 2oc2: Structure of Testis Ace with RXPA380

Enzymatic activity of Structure of Testis Ace with RXPA380

All present enzymatic activity of Structure of Testis Ace with RXPA380:
3.4.15.1;

Protein crystallography data

The structure of Structure of Testis Ace with RXPA380, PDB code: 2oc2 was solved by H.R.Corradi, C.S.Anthony, S.L.Schwager, P.Redelinghuys, D.Georgiadis, V.Dive, K.R.Acharya, E.D.Sturrock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.12 / 2.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.514, 84.763, 133.483, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 26.2

Other elements in 2oc2:

The structure of Structure of Testis Ace with RXPA380 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Testis Ace with RXPA380 (pdb code 2oc2). 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 Structure of Testis Ace with RXPA380, PDB code: 2oc2:

Zinc binding site 1 out of 1 in 2oc2

Go back to Zinc Binding Sites List in 2oc2
Zinc binding site 1 out of 1 in the Structure of Testis Ace with RXPA380


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Testis Ace with RXPA380 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:17.9
occ:1.00
OE1 A:GLU411 1.9 13.9 1.0
O3 A:RX3680 2.0 16.4 1.0
NE2 A:HIS383 2.0 14.6 1.0
NE2 A:HIS387 2.0 13.0 1.0
O4 A:RX3680 2.5 17.2 1.0
P1 A:RX3680 2.7 17.3 1.0
CD2 A:HIS383 2.9 13.9 1.0
CE1 A:HIS387 2.9 12.7 1.0
CD A:GLU411 3.0 13.6 1.0
CE1 A:HIS383 3.0 13.0 1.0
CD2 A:HIS387 3.1 13.7 1.0
OE2 A:GLU411 3.4 11.5 1.0
C17 A:RX3680 3.7 16.0 1.0
C9 A:RX3680 3.9 16.5 1.0
C18 A:RX3680 3.9 15.6 1.0
CG A:HIS383 4.0 13.9 1.0
N1 A:RX3680 4.0 17.0 1.0
ND1 A:HIS383 4.0 12.5 1.0
ND1 A:HIS387 4.1 13.8 1.0
CE2 A:TYR523 4.1 10.5 1.0
CG A:HIS387 4.2 14.2 1.0
CG A:GLU411 4.3 13.0 1.0
OH A:TYR523 4.3 9.9 1.0
C1 A:RX3680 4.4 17.6 1.0
OE2 A:GLU384 4.4 18.0 1.0
CB A:GLU411 4.5 13.9 1.0
CA A:GLU411 4.5 14.1 1.0
O2 A:RX3680 4.6 18.6 1.0
CZ A:TYR523 4.7 10.5 1.0
C19 A:RX3680 4.8 16.8 1.0

Reference:

C.S.Anthony, H.R.Corradi, S.L.Schwager, P.Redelinghuys, D.Georgiadis, V.Dive, K.R.Acharya, E.D.Sturrock. The N Domain of Human Angiotensin-I Converting Enzyme: the Role of N-Glycosylation and the Crystal Structure in Complex with An N Domain Specific Phosphinic Inhibitor RXP407. J.Biol.Chem. V. 46 5473 2010.
ISSN: ISSN 0021-9258
PubMed: 20826823
DOI: 10.1074/JBC.M110.167866
Page generated: Wed Dec 16 03:45:48 2020

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