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Zinc in PDB 2fhx: Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase

Enzymatic activity of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase

All present enzymatic activity of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase:
3.5.2.6;

Protein crystallography data

The structure of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase, PDB code: 2fhx was solved by T.A.Murphy, L.E.Catto, S.E.Halford, A.T.Hadfield, W.Minor, T.R.Walsh, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 126.936, 126.936, 90.461, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 24.7

Other elements in 2fhx:

The structure of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase (pdb code 2fhx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase, PDB code: 2fhx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2fhx

Go back to Zinc Binding Sites List in 2fhx
Zinc binding site 1 out of 2 in the Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn317

b:20.9
occ:1.00
O A:HOH710 1.7 27.4 1.0
NE2 A:HIS196 2.0 17.4 1.0
ND1 A:HIS118 2.1 19.1 1.0
NE2 A:HIS116 2.2 15.8 1.0
CD2 A:HIS196 2.9 15.8 1.0
CD2 A:HIS116 3.0 14.8 1.0
O A:HOH594 3.0 25.8 1.0
CE1 A:HIS118 3.0 19.2 1.0
CG A:HIS118 3.1 17.9 1.0
CE1 A:HIS196 3.1 16.6 1.0
CE1 A:HIS116 3.3 16.3 1.0
OD2 A:CSD221 3.3 35.1 1.0
CB A:HIS118 3.4 17.4 1.0
OD2 A:ASP120 3.9 27.1 1.0
CG A:HIS196 4.1 16.1 1.0
NE2 A:HIS118 4.1 18.1 1.0
ND1 A:HIS196 4.2 16.1 1.0
CD2 A:HIS118 4.2 17.6 1.0
CG A:HIS116 4.2 16.6 1.0
ND1 A:HIS116 4.3 16.5 1.0
SG A:CSD221 4.3 31.6 1.0
N3 A:AZI401 4.4 35.8 1.0
CB A:CSD221 4.4 22.7 1.0
OD1 A:ASP120 4.4 26.4 1.0
O B:HOH658 4.4 43.6 1.0
CG A:ASP120 4.6 24.1 1.0
O B:HOH608 4.7 33.4 1.0
CA A:HIS118 4.8 17.3 1.0
N2 A:AZI401 4.9 32.5 1.0

Zinc binding site 2 out of 2 in 2fhx

Go back to Zinc Binding Sites List in 2fhx
Zinc binding site 2 out of 2 in the Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn317

b:25.7
occ:1.00
O B:HOH728 1.8 36.3 1.0
NE2 B:HIS196 2.1 20.8 1.0
ND1 B:HIS118 2.1 21.8 1.0
NE2 B:HIS116 2.2 24.2 1.0
CD2 B:HIS196 3.0 19.8 1.0
O B:HOH664 3.0 28.8 1.0
CD2 B:HIS116 3.1 24.9 1.0
CE1 B:HIS118 3.1 21.4 1.0
CE1 B:HIS196 3.1 20.7 1.0
CG B:HIS118 3.1 23.3 1.0
CE1 B:HIS116 3.3 25.9 1.0
CB B:HIS118 3.4 23.8 1.0
OD2 B:ASP120 3.9 30.1 1.0
CG B:HIS196 4.2 20.6 1.0
ND1 B:HIS196 4.2 21.1 1.0
NE2 B:HIS118 4.2 22.8 1.0
CD2 B:HIS118 4.2 22.1 1.0
CG B:HIS116 4.3 25.9 1.0
N1 B:AZI402 4.3 37.4 1.0
ND1 B:HIS116 4.3 25.3 1.0
SG B:CSO221 4.3 35.6 1.0
OD1 B:ASP120 4.4 30.5 1.0
CB B:CSO221 4.4 29.4 1.0
CG B:ASP120 4.5 30.0 1.0
O A:HOH649 4.6 51.8 1.0
O A:HOH523 4.9 32.9 1.0
N2 B:AZI402 4.9 31.5 1.0
CA B:HIS118 4.9 24.1 1.0

Reference:

T.A.Murphy, L.E.Catto, S.E.Halford, A.T.Hadfield, W.Minor, T.R.Walsh, J.Spencer. Crystal Structure of Pseudomonas Aeruginosa Spm-1 Provides Insights Into Variable Zinc Affinity of Metallo-Beta-Lactamases. J.Mol.Biol. V. 357 890 2006.
ISSN: ISSN 0022-2836
PubMed: 16460758
DOI: 10.1016/J.JMB.2006.01.003
Page generated: Wed Dec 16 03:28:11 2020

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