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Zinc in PDB 2bn7: Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn

Enzymatic activity of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn

All present enzymatic activity of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn:
3.4.11.9;

Protein crystallography data

The structure of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn, PDB code: 2bn7 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) 119.52 / 2.40
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 139.695, 139.695, 230.674, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 18.7

Other elements in 2bn7:

The structure of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Manganese (Mn) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn (pdb code 2bn7). 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 Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn, PDB code: 2bn7:

Zinc binding site 1 out of 1 in 2bn7

Go back to Zinc Binding Sites List in 2bn7
Zinc binding site 1 out of 1 in the Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1445

b:70.4
occ:0.75
 O A:PRO501 2.5 54.5 1.0
NE2 A:HIS361 2.5 56.5 1.0
N A:PRO501 2.5 53.8 1.0
NE2 A:HIS243 2.6 66.0 1.0
CE1 A:HIS361 2.7 60.9 1.0
O A:HOH2286 2.9 58.6 1.0
C A:PRO501 3.1 54.4 1.0
CA A:PRO501 3.3 54.1 1.0
CD2 A:HIS243 3.4 66.6 1.0
CD A:PRO501 3.5 53.3 1.0
CE1 A:HIS243 3.7 67.2 1.0
O A:HOH2284 3.7 42.8 1.0
CD2 A:HIS361 3.8 56.6 1.0
ND1 A:HIS361 4.1 62.2 1.0
N A:LEU502 4.3 54.8 1.0
CB A:PRO501 4.5 54.3 1.0
CG A:HIS361 4.6 55.6 1.0
CG A:HIS243 4.6 63.9 1.0
CG A:PRO501 4.7 53.8 1.0
ND1 A:HIS243 4.7 68.2 1.0
MN A:MN1441 4.9 41.9 1.0
NE2 A:HIS354 4.9 52.6 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: Wed Dec 16 03:18:34 2020

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