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Nickel in PDB 2ai7: S.Pneumoniae Polypeptide Deformylase Complexed with Sb- 485345

Enzymatic activity of S.Pneumoniae Polypeptide Deformylase Complexed with Sb- 485345

All present enzymatic activity of S.Pneumoniae Polypeptide Deformylase Complexed with Sb- 485345:
3.5.1.88;

Protein crystallography data

The structure of S.Pneumoniae Polypeptide Deformylase Complexed with Sb- 485345, PDB code: 2ai7 was solved by K.J.Smith, C.M.Petit, K.Aubart, M.Smyth, E.Mcmanus, J.Jones, A.Fosberry, C.Lewis, M.Lonetto, S.B.Christensen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 49.889, 49.889, 91.565, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 26.3

Nickel Binding Sites:

The binding sites of Nickel atom in the S.Pneumoniae Polypeptide Deformylase Complexed with Sb- 485345 (pdb code 2ai7). 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 S.Pneumoniae Polypeptide Deformylase Complexed with Sb- 485345, PDB code: 2ai7:

Nickel binding site 1 out of 1 in 2ai7

Go back to Nickel Binding Sites List in 2ai7
Nickel binding site 1 out of 1 in the S.Pneumoniae Polypeptide Deformylase Complexed with Sb- 485345


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of S.Pneumoniae Polypeptide Deformylase Complexed with Sb- 485345 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni301

b:38.9
occ:1.00
NE2 A:HIS177 2.2 25.4 1.0
NE2 A:HIS173 2.2 29.8 1.0
O25 A:SB7300 2.4 25.6 1.0
SG A:CYS130 2.5 28.1 1.0
O22 A:SB7300 2.5 35.3 1.0
C24 A:SB7300 2.9 29.8 1.0
N14 A:SB7300 2.9 33.3 1.0
CD2 A:HIS173 3.1 27.6 1.0
CE1 A:HIS177 3.1 24.0 1.0
CD2 A:HIS177 3.2 24.6 1.0
CE1 A:HIS173 3.2 30.5 1.0
NE2 A:GLN76 3.4 24.4 1.0
CB A:CYS130 3.5 31.0 1.0
O A:HOH3039 3.6 23.4 1.0
CA A:CYS130 3.9 30.2 1.0
CD A:GLN76 4.0 25.0 1.0
OE1 A:GLN76 4.2 23.6 1.0
C11 A:SB7300 4.2 35.2 1.0
ND1 A:HIS177 4.3 26.5 1.0
CG A:HIS173 4.3 26.5 1.0
N A:LEU131 4.3 30.7 1.0
ND1 A:HIS173 4.3 28.5 1.0
CG A:HIS177 4.3 24.0 1.0
C8 A:SB7300 4.5 38.6 1.0
C A:CYS130 4.6 31.6 1.0
O A:HOH3009 4.6 23.1 1.0
O A:GLY129 4.7 29.9 1.0
OE1 A:GLU174 4.8 21.2 1.0
OE2 A:GLU174 4.8 25.7 1.0

Reference:

K.J.Smith, C.M.Petit, K.Aubart, M.Smyth, E.Mcmanus, J.Jones, A.Fosberry, C.Lewis, M.Lonetto, S.B.Christensen. Structural Variation and Inhibitor Binding in Polypeptide Deformylase From Four Different Bacterial Species Protein Sci. V. 12 349 2003.
ISSN: ISSN 0961-8368
PubMed: 12538898
DOI: 10.1110/PS.0229303
Page generated: Fri Sep 25 08:05:42 2020
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