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Nickel in PDB 5d7z: Crystal Structure of Glyoxalase I From Zea Mays

Enzymatic activity of Crystal Structure of Glyoxalase I From Zea Mays

All present enzymatic activity of Crystal Structure of Glyoxalase I From Zea Mays:
4.4.1.5;

Protein crystallography data

The structure of Crystal Structure of Glyoxalase I From Zea Mays, PDB code: 5d7z was solved by J.M.Gonzalez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.80 / 1.73
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 90.690, 90.690, 74.713, 90.00, 90.00, 120.00
R / Rfree (%) 16.6 / 20.2

Other elements in 5d7z:

The structure of Crystal Structure of Glyoxalase I From Zea Mays also contains other interesting chemical elements:

Sodium (Na) 1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of Glyoxalase I From Zea Mays (pdb code 5d7z). 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 Glyoxalase I From Zea Mays, PDB code: 5d7z:

Nickel binding site 1 out of 1 in 5d7z

Go back to Nickel Binding Sites List in 5d7z
Nickel binding site 1 out of 1 in the Crystal Structure of Glyoxalase I From Zea Mays


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 Glyoxalase I From Zea Mays within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni301

b:24.9
occ:0.33
NE2 A:HIS290 2.1 25.6 1.0
NE2 A:HIS295 2.1 27.0 1.0
CE1 A:HIS290 3.1 21.8 1.0
CD2 A:HIS295 3.1 27.7 1.0
CE1 A:HIS295 3.1 29.2 1.0
CD2 A:HIS290 3.2 23.3 1.0
ND1 A:HIS290 4.2 25.0 1.0
ND1 A:HIS295 4.2 31.2 1.0
CG A:HIS295 4.3 28.0 1.0
CG A:HIS290 4.3 22.7 1.0

Reference:

G.L.Turra, R.B.Agostini, C.M.Fauguel, D.A.Presello, C.S.Andreo, J.M.Gonzalez, V.A.Campos-Bermudez. Structure of the Novel Monomeric Glyoxalase I From Zea Mays. Acta Crystallogr.,Sect.D V. 71 2009 2015.
ISSN: ESSN 1399-0047
PubMed: 26457425
DOI: 10.1107/S1399004715015205
Page generated: Wed Dec 16 01:40:28 2020

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