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Nickel in PDB 8izu: Crystal Structure of the N-Terminal Domain (Residues 1-137) of Mpxv A7

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Domain (Residues 1-137) of Mpxv A7, PDB code: 8izu was solved by X.C.Ni, J.Lei, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.45 / 2.54
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 37.903, 140.327, 153.519, 90, 90, 90
R / Rfree (%) 20.1 / 23.8

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of the N-Terminal Domain (Residues 1-137) of Mpxv A7 (pdb code 8izu). 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 the N-Terminal Domain (Residues 1-137) of Mpxv A7, PDB code: 8izu:

Nickel binding site 1 out of 1 in 8izu

Go back to Nickel Binding Sites List in 8izu
Nickel binding site 1 out of 1 in the Crystal Structure of the N-Terminal Domain (Residues 1-137) of Mpxv A7


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 the N-Terminal Domain (Residues 1-137) of Mpxv A7 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni202

b:107.6
occ:1.00
O B:HOH205 2.8 47.4 1.0
O A:HOH311 3.2 49.0 1.0
NH1 B:ARG21 3.3 52.1 1.0
OD2 A:ASP17 3.4 63.3 1.0
NH1 A:ARG21 3.9 38.3 0.6
OE2 A:GLU96 3.9 56.9 1.0
OE2 B:GLU96 4.2 74.6 1.0
O B:LYS91 4.2 50.2 1.0
OD1 A:ASN18 4.3 57.3 1.0
OD2 B:ASP93 4.3 49.5 1.0
O A:HOH312 4.5 53.5 1.0
N B:ASP93 4.5 49.4 1.0
CG A:ASP17 4.5 56.6 1.0
CZ B:ARG21 4.6 53.5 1.0
CA B:LEU92 4.6 48.0 1.0
ND2 A:ASN18 4.7 40.0 1.0
CD2 A:LEU92 4.8 52.1 1.0
ND2 B:ASN18 4.9 46.7 1.0
CZ A:ARG21 4.9 35.7 0.6
CG A:ASN18 4.9 44.9 1.0
CD2 B:LEU92 4.9 50.2 1.0
O A:LYS91 5.0 49.1 1.0

Reference:

X.C.Ni, J.Lei. Crystal Structure of the N-Terminal Domain (Residues 1-137) of Mpxv A7 To Be Published.
Page generated: Thu Oct 10 09:43:04 2024

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