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Nickel in PDB 5ht8: Crystal Structure of Clostrillin Double Mutant (S17H,S19H) in Complex with Nickel

Protein crystallography data

The structure of Crystal Structure of Clostrillin Double Mutant (S17H,S19H) in Complex with Nickel, PDB code: 5ht8 was solved by A.Jamkhindikar, S.S.Srivastava, R.Sankaranarayanan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.57 / 2.01
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 77.687, 77.687, 74.623, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 23.6

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of Clostrillin Double Mutant (S17H,S19H) in Complex with Nickel (pdb code 5ht8). 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 Clostrillin Double Mutant (S17H,S19H) in Complex with Nickel, PDB code: 5ht8:

Nickel binding site 1 out of 1 in 5ht8

Go back to Nickel Binding Sites List in 5ht8
Nickel binding site 1 out of 1 in the Crystal Structure of Clostrillin Double Mutant (S17H,S19H) in Complex with Nickel


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 Clostrillin Double Mutant (S17H,S19H) in Complex with Nickel within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni101

b:41.8
occ:1.00
O A:HOH210 1.8 29.4 1.0
NE2 A:HIS19 2.1 31.2 1.0
NE2 A:HIS17 2.2 31.7 1.0
O A:HOH231 2.3 32.5 1.0
O A:HOH236 2.4 36.6 1.0
O A:HOH234 2.4 30.2 1.0
CE1 A:HIS19 3.0 30.0 1.0
CD2 A:HIS17 3.1 29.3 1.0
CD2 A:HIS19 3.2 28.4 1.0
CE1 A:HIS17 3.2 29.4 1.0
ND1 A:HIS19 4.1 31.0 1.0
CG A:HIS17 4.2 29.1 1.0
CG A:HIS19 4.3 31.0 1.0
ND1 A:HIS17 4.3 28.3 1.0

Reference:

S.S.Srivastava, A.A.Jamkhindikar, R.Raman, M.K.Jobby, S.Chadalawada, R.Sankaranarayanan, Y.Sharma. A Transition Metal-Binding, Trimeric Beta Gamma-Crystallin From Methane-Producing Thermophilic Archaea, Methanosaeta Thermophila Biochemistry V. 56 1299 2017.
ISSN: ISSN 1520-4995
PubMed: 28029780
DOI: 10.1021/ACS.BIOCHEM.6B00985
Page generated: Thu Oct 10 06:28:00 2024

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