Atomistry » Zinc » PDB 1w56-1wfl » 1wbq
Atomistry »
  Zinc »
    PDB 1w56-1wfl »
      1wbq »

Zinc in PDB 1wbq: Znmg Substituted Aminopeptidase P From E. Coli

Enzymatic activity of Znmg Substituted Aminopeptidase P From E. Coli

All present enzymatic activity of Znmg Substituted Aminopeptidase P From E. Coli:
3.4.11.9;

Protein crystallography data

The structure of Znmg Substituted Aminopeptidase P From E. Coli, PDB code: 1wbq was solved by S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.97 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 111.974, 236.703, 137.637, 90.00, 106.14, 90.00
R / Rfree (%) 16.7 / 19.7

Other elements in 1wbq:

The structure of Znmg Substituted Aminopeptidase P From E. Coli also contains other interesting chemical elements:

Magnesium (Mg) 6 atoms
Chlorine (Cl) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Znmg Substituted Aminopeptidase P From E. Coli (pdb code 1wbq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Znmg Substituted Aminopeptidase P From E. Coli, PDB code: 1wbq:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1wbq

Go back to Zinc Binding Sites List in 1wbq
Zinc binding site 1 out of 4 in the Znmg Substituted Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Znmg Substituted Aminopeptidase P From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1440

b:53.9
occ:1.00
OE2 A:GLU406 2.2 44.6 1.0
OD2 A:ASP271 2.2 35.7 1.0
NE2 A:HIS354 2.2 30.8 1.0
O A:HOH2191 2.4 37.8 1.0
OE2 A:GLU383 2.5 41.5 1.0
CG A:ASP271 3.0 32.7 1.0
CE1 A:HIS354 3.2 31.0 1.0
CD A:GLU406 3.2 33.5 1.0
O A:HOH2155 3.2 45.7 1.0
CD A:GLU383 3.2 36.4 1.0
CD2 A:HIS354 3.2 28.8 1.0
OD1 A:ASP271 3.2 29.9 1.0
OE1 A:GLU383 3.3 40.1 1.0
MG A:MG1441 3.3 32.0 1.0
OE1 A:GLU406 3.5 32.2 1.0
CG2 A:THR381 3.7 30.5 1.0
OG1 A:THR381 3.8 30.6 1.0
O A:HOH2134 3.8 34.0 1.0
CB A:THR381 4.0 30.7 1.0
ND1 A:HIS354 4.3 32.6 1.0
CB A:ASP271 4.3 32.7 1.0
CG A:HIS354 4.3 34.6 1.0
CG A:GLU406 4.5 35.0 1.0
CG A:GLU383 4.5 36.9 1.0
NE2 A:HIS361 4.8 39.6 1.0
CD2 A:HIS361 5.0 42.4 1.0
CG2 A:VAL360 5.0 35.5 1.0

Zinc binding site 2 out of 4 in 1wbq

Go back to Zinc Binding Sites List in 1wbq
Zinc binding site 2 out of 4 in the Znmg Substituted Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Znmg Substituted Aminopeptidase P From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1440

b:44.1
occ:1.00
OE2 B:GLU406 2.2 43.0 1.0
OD2 B:ASP271 2.2 32.5 1.0
NE2 B:HIS354 2.3 30.6 1.0
O B:HOH2285 2.3 24.2 1.0
OE2 B:GLU383 2.5 43.3 1.0
CG B:ASP271 3.0 31.2 1.0
CD B:GLU406 3.1 34.9 1.0
CD B:GLU383 3.2 37.3 1.0
OE1 B:GLU383 3.2 40.6 1.0
CD2 B:HIS354 3.2 26.5 1.0
MG B:MG1441 3.2 26.7 1.0
CE1 B:HIS354 3.3 29.1 1.0
OD1 B:ASP271 3.3 32.0 1.0
O B:HOH2235 3.3 34.9 1.0
OE1 B:GLU406 3.4 31.6 1.0
CG2 B:THR381 3.7 31.9 1.0
O B:HOH2198 3.8 25.8 1.0
OG1 B:THR381 3.8 28.7 1.0
CB B:THR381 4.0 30.6 1.0
CB B:ASP271 4.3 33.8 1.0
CG B:HIS354 4.4 33.7 1.0
ND1 B:HIS354 4.4 30.2 1.0
CG B:GLU406 4.5 34.7 1.0
CG B:GLU383 4.5 37.2 1.0
NE2 B:HIS361 4.8 38.7 1.0
CG2 B:VAL360 4.9 36.0 1.0
CD2 B:HIS361 5.0 41.2 1.0

Zinc binding site 3 out of 4 in 1wbq

Go back to Zinc Binding Sites List in 1wbq
Zinc binding site 3 out of 4 in the Znmg Substituted Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Znmg Substituted Aminopeptidase P From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1440

b:67.0
occ:1.00
OD2 C:ASP271 2.1 30.5 1.0
OE2 C:GLU406 2.2 43.1 1.0
NE2 C:HIS354 2.3 31.4 1.0
OE2 C:GLU383 2.4 42.3 1.0
CD C:GLU383 3.0 36.5 1.0
CG C:ASP271 3.1 31.8 1.0
CD C:GLU406 3.1 33.7 1.0
MG C:MG1441 3.1 60.4 1.0
OE1 C:GLU383 3.2 42.8 1.0
CD2 C:HIS354 3.2 28.1 1.0
CE1 C:HIS354 3.2 30.6 1.0
OE1 C:GLU406 3.3 31.2 1.0
OD1 C:ASP271 3.4 32.6 1.0
CG2 C:THR381 3.7 30.8 1.0
OG1 C:THR381 3.7 28.3 1.0
CB C:THR381 3.9 29.4 1.0
CB C:ASP271 4.3 30.9 1.0
ND1 C:HIS354 4.3 32.5 1.0
CG C:GLU383 4.4 36.3 1.0
CG C:HIS354 4.4 34.2 1.0
CG C:GLU406 4.4 34.8 1.0
NE2 C:HIS361 4.9 36.6 1.0
CB C:GLU383 5.0 35.6 1.0

Zinc binding site 4 out of 4 in 1wbq

Go back to Zinc Binding Sites List in 1wbq
Zinc binding site 4 out of 4 in the Znmg Substituted Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Znmg Substituted Aminopeptidase P From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1440

b:46.7
occ:1.00
OE2 D:GLU406 2.1 44.5 1.0
OD2 D:ASP271 2.1 35.8 1.0
NE2 D:HIS354 2.3 31.5 1.0
O D:HOH2256 2.3 25.0 1.0
OE2 D:GLU383 2.5 43.2 1.0
CG D:ASP271 3.0 31.1 1.0
CD D:GLU406 3.1 35.4 1.0
CD D:GLU383 3.2 34.8 1.0
CD2 D:HIS354 3.2 26.4 1.0
OE1 D:GLU383 3.2 40.9 1.0
CE1 D:HIS354 3.2 31.3 1.0
OD1 D:ASP271 3.3 30.4 1.0
MG D:MG1441 3.3 29.7 1.0
OE1 D:GLU406 3.4 31.3 1.0
CG2 D:THR381 3.7 31.1 1.0
OG1 D:THR381 3.9 28.8 1.0
CB D:THR381 4.0 29.1 1.0
O D:HOH2172 4.1 25.5 1.0
CB D:ASP271 4.3 32.3 1.0
ND1 D:HIS354 4.3 33.1 1.0
CG D:HIS354 4.3 35.9 1.0
CG D:GLU406 4.4 33.9 1.0
CG D:GLU383 4.5 37.7 1.0
NE2 D:HIS361 4.9 40.6 1.0
CG2 D:VAL360 4.9 36.3 1.0

Reference:

S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss. Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, A Metalloprotease with A Dinuclear Metal Center. Biochemistry V. 44 13820 2005.
ISSN: ISSN 0006-2960
PubMed: 16229471
DOI: 10.1021/BI0512849
Page generated: Mon Jan 25 16:15:29 2021

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