Atomistry » Zinc » PDB 2zen-2zws » 2zo4
Atomistry »
  Zinc »
    PDB 2zen-2zws »
      2zo4 »

Zinc in PDB 2zo4: Crystal Structure of Metallo-Beta-Lactamase Family Protein TTHA1429 From Thermus Thermophilus HB8

Protein crystallography data

The structure of Crystal Structure of Metallo-Beta-Lactamase Family Protein TTHA1429 From Thermus Thermophilus HB8, PDB code: 2zo4 was solved by A.Yamamura, K.Nagata, Y.Agari, A.Ebihara, N.Nakagawa, S.Yokoyama, S.Kuramitsu, M.Tanokura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.286, 62.885, 87.425, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 25.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Metallo-Beta-Lactamase Family Protein TTHA1429 From Thermus Thermophilus HB8 (pdb code 2zo4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Metallo-Beta-Lactamase Family Protein TTHA1429 From Thermus Thermophilus HB8, PDB code: 2zo4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2zo4

Go back to Zinc Binding Sites List in 2zo4
Zinc binding site 1 out of 2 in the Crystal Structure of Metallo-Beta-Lactamase Family Protein TTHA1429 From Thermus Thermophilus HB8


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 Metallo-Beta-Lactamase Family Protein TTHA1429 From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn318

b:14.6
occ:1.00
O A:HOH320 2.0 8.0 1.0
NE2 A:HIS171 2.1 11.2 1.0
ND1 A:HIS72 2.2 10.5 1.0
NE2 A:HIS70 2.2 9.3 1.0
OD2 A:ASP190 2.6 11.9 1.0
CD2 A:HIS171 3.0 9.9 1.0
CD2 A:HIS70 3.0 8.0 1.0
CE1 A:HIS171 3.1 10.6 1.0
CE1 A:HIS72 3.2 11.1 1.0
CG A:HIS72 3.2 10.1 1.0
ZN A:ZN319 3.3 14.2 1.0
CE1 A:HIS70 3.3 8.3 1.0
CB A:HIS72 3.5 10.0 1.0
CG A:ASP190 3.5 11.5 1.0
CB A:ASP190 3.8 11.2 1.0
NE2 A:HIS75 4.1 9.9 1.0
CD2 A:HIS75 4.1 9.5 1.0
CG A:HIS171 4.2 10.0 1.0
ND1 A:HIS171 4.2 10.6 1.0
CG A:HIS70 4.2 8.3 1.0
NE2 A:HIS72 4.3 10.7 1.0
CD2 A:HIS72 4.3 10.8 1.0
ND1 A:HIS70 4.4 7.8 1.0
OD1 A:ASP74 4.5 12.5 1.0
OD1 A:ASP190 4.6 11.3 1.0
OD2 A:ASP74 4.7 12.3 1.0
CA A:HIS72 5.0 9.8 1.0
O A:HOH527 5.0 58.2 1.0

Zinc binding site 2 out of 2 in 2zo4

Go back to Zinc Binding Sites List in 2zo4
Zinc binding site 2 out of 2 in the Crystal Structure of Metallo-Beta-Lactamase Family Protein TTHA1429 From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Metallo-Beta-Lactamase Family Protein TTHA1429 From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn319

b:14.2
occ:1.00
O A:HOH320 2.0 8.0 1.0
NE2 A:HIS75 2.1 9.9 1.0
OD2 A:ASP190 2.1 11.9 1.0
NE2 A:HIS233 2.1 13.8 1.0
OD2 A:ASP74 2.3 12.3 1.0
CD2 A:HIS75 2.9 9.5 1.0
CG A:ASP190 3.0 11.5 1.0
CD2 A:HIS233 3.0 13.4 1.0
CE1 A:HIS233 3.1 13.8 1.0
CE1 A:HIS75 3.2 8.8 1.0
OD1 A:ASP190 3.2 11.3 1.0
ZN A:ZN318 3.3 14.6 1.0
CG A:ASP74 3.3 12.3 1.0
OD1 A:ASP74 3.7 12.5 1.0
NE2 A:HIS70 4.1 9.3 1.0
CG A:HIS75 4.1 10.0 1.0
ND1 A:HIS233 4.2 13.5 1.0
CG A:HIS233 4.2 13.3 1.0
ND1 A:HIS75 4.2 8.9 1.0
CE1 A:HIS70 4.3 8.3 1.0
CB A:ASP190 4.4 11.2 1.0
O A:HOH455 4.5 28.1 1.0
CB A:ASP74 4.6 11.2 1.0
CG2 A:VAL22 4.7 15.1 1.0
NE2 A:HIS171 4.8 11.2 1.0

Reference:

A.Yamamura, J.Ohtsuka, K.Kubota, Y.Agari, A.Ebihara, N.Nakagawa, K.Nagata, M.Tanokura. Crystal Structure of TTHA1429, A Novel Metallo-Beta-Lactamase Superfamily Protein From Thermus Thermophilus HB8. Proteins V. 73 1053 2008.
ISSN: ISSN 0887-3585
PubMed: 18767153
DOI: 10.1002/PROT.22215
Page generated: Wed Dec 16 04:05:31 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy