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Mercury in PDB 1kgz: Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum)

Enzymatic activity of Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum)

All present enzymatic activity of Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum):
2.4.2.18;

Protein crystallography data

The structure of Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum), PDB code: 1kgz was solved by C.Kim, N.-H.Xuong, S.Edwards, Madhusudan, M.-C.Yee, G.Spraggon, S.E.Mills, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.40
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.378, 81.686, 101.680, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 26.5

Other elements in 1kgz:

The structure of Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum) also contains other interesting chemical elements:

Manganese (Mn) 4 atoms

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum) (pdb code 1kgz). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum), PDB code: 1kgz:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 1kgz

Go back to Mercury Binding Sites List in 1kgz
Mercury binding site 1 out of 2 in the Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg400

b:57.5
occ:1.00
 O A:CYS113 2.4 30.8 1.0
SG A:CYS113 2.6 46.4 1.0
CB A:CYS113 3.2 39.5 1.0
C A:CYS113 3.3 40.0 1.0
CD1 A:LEU310 3.4 32.7 1.0
CA A:CYS113 3.6 38.8 1.0
CD1 A:LEU324 4.1 27.1 1.0
CD2 A:LEU310 4.1 33.9 1.0
CB A:LEU324 4.2 30.1 1.0
CG A:LEU310 4.4 39.9 1.0
N A:GLY114 4.5 41.4 1.0
CG A:LEU324 4.8 34.5 1.0
N A:CYS113 5.0 41.8 1.0

Mercury binding site 2 out of 2 in 1kgz

Go back to Mercury Binding Sites List in 1kgz
Mercury binding site 2 out of 2 in the Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase From Erwinia Carotovora (Current Name, Pectobacterium Carotovorum) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg400

b:44.7
occ:1.00
 SG B:CYS113 2.4 32.9 1.0
O B:CYS113 2.7 38.0 1.0
C B:CYS113 3.2 34.8 1.0
CB B:CYS113 3.4 34.0 1.0
CD2 B:LEU310 3.5 27.4 1.0
CA B:CYS113 3.9 32.4 1.0
N B:GLY114 3.9 35.2 1.0
N B:ALA115 3.9 36.6 1.0
CD1 B:LEU310 3.9 29.5 1.0
O B:ALA110 4.1 41.0 1.0
CA B:GLY114 4.2 35.2 1.0
CD2 B:LEU324 4.3 27.2 1.0
C B:GLY114 4.3 36.4 1.0
CG B:LEU310 4.3 28.0 1.0
CB B:ALA115 4.4 30.8 1.0
CA B:ALA115 4.7 35.9 1.0
N B:CYS113 4.7 36.7 1.0

Reference:

C.Kim, N.-H.Xuong, S.Edwards, Madhusudan, M.-C.Yee, G.Spraggon, S.E.Mills. The Crystal Structure of Anthranilate Phosphoribosyltransferase From the Enterobacterium Pectobacterium Carotovorum Febs Lett. V. 523 239 2002.
ISSN: ISSN 0014-5793
PubMed: 12123839
DOI: 10.1016/S0014-5793(02)02905-8
Page generated: Sun Aug 11 00:20:41 2024

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