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Nickel in PDB 1ns2: Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304A Complexed with Galactose

Enzymatic activity of Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304A Complexed with Galactose

All present enzymatic activity of Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304A Complexed with Galactose:
5.1.3.3;

Protein crystallography data

The structure of Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304A Complexed with Galactose, PDB code: 1ns2 was solved by H.M.Holden, J.B.Thoden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.800, 76.400, 211.400, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 21.6

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304A Complexed with Galactose (pdb code 1ns2). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304A Complexed with Galactose, PDB code: 1ns2:

Nickel binding site 1 out of 1 in 1ns2

Go back to Nickel Binding Sites List in 1ns2
Nickel binding site 1 out of 1 in the Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304A Complexed with Galactose


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304A Complexed with Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni1401

b:28.8
occ:1.00
OD1 A:ASP13 2.4 20.1 1.0
OD1 B:ASP13 2.4 20.6 1.0
O A:HOH1404 2.4 16.3 1.0
O B:HOH2505 2.5 16.9 1.0
O A:HOH1533 2.5 44.0 1.0
CG A:ASP13 3.1 29.7 1.0
CG B:ASP13 3.1 15.8 1.0
OD2 A:ASP13 3.2 22.0 1.0
OD2 B:ASP13 3.3 16.3 1.0
O A:SER12 4.2 19.5 1.0
O B:SER12 4.4 17.1 1.0
CB A:ASP13 4.5 12.5 1.0
O B:GLY11 4.5 21.8 1.0
CB B:ASP13 4.5 18.7 1.0
O A:GLY11 4.6 29.6 1.0
C A:SER12 4.6 22.5 1.0
CA B:ASP7 4.7 15.9 1.0
CA A:ASP13 4.7 11.0 1.0
C B:SER12 4.8 15.7 1.0
CB B:ASP7 4.8 18.0 1.0
CA B:ASP13 4.8 15.4 1.0
N A:ASP13 4.8 13.2 1.0
CA A:ASP7 4.9 21.6 1.0
N B:ASP13 5.0 18.9 1.0
N B:ASP7 5.0 18.4 1.0

Reference:

J.B.Thoden, J.Kim, F.M.Raushel, H.M.Holden. The Catalytic Mechanism of Galactose Mutarotase Protein Sci. V. 12 1051 2003.
ISSN: ISSN 0961-8368
PubMed: 12717027
DOI: 10.1110/PS.0243203
Page generated: Fri Sep 25 07:57:19 2020
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