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Nickel in PDB 2aia: S.Pneumoniae Pdf Complexed with Sb-543668

Enzymatic activity of S.Pneumoniae Pdf Complexed with Sb-543668

All present enzymatic activity of S.Pneumoniae Pdf Complexed with Sb-543668:
3.5.1.88;

Protein crystallography data

The structure of S.Pneumoniae Pdf Complexed with Sb-543668, PDB code: 2aia 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 / 1.70
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 49.701, 49.701, 91.835, 90.00, 90.00, 90.00
R / Rfree (%) 23.5 / 26.8

Nickel Binding Sites:

The binding sites of Nickel atom in the S.Pneumoniae Pdf Complexed with Sb-543668 (pdb code 2aia). 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 Pdf Complexed with Sb-543668, PDB code: 2aia:

Nickel binding site 1 out of 1 in 2aia

Go back to Nickel Binding Sites List in 2aia
Nickel binding site 1 out of 1 in the S.Pneumoniae Pdf Complexed with Sb-543668


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of S.Pneumoniae Pdf Complexed with Sb-543668 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni601

b:36.4
occ:1.00
NE2 A:HIS177 2.2 25.1 1.0
O32 A:SB8501 2.2 40.3 0.5
NE2 A:HIS173 2.2 25.9 1.0
O35 A:SB8501 2.3 22.1 0.5
O35 A:SB8501 2.3 28.4 0.5
SG A:CYS130 2.4 28.3 1.0
O32 A:SB8501 2.6 36.0 0.5
N29 A:SB8501 2.8 39.7 0.5
C34 A:SB8501 2.8 31.3 0.5
C34 A:SB8501 2.9 33.4 0.5
N29 A:SB8501 3.0 35.3 0.5
CD2 A:HIS173 3.1 28.3 1.0
CE1 A:HIS177 3.1 18.7 1.0
CD2 A:HIS177 3.1 16.6 1.0
CE1 A:HIS173 3.2 30.3 1.0
NE2 A:GLN76 3.5 25.7 1.0
CB A:CYS130 3.6 28.9 1.0
O A:HOH3039 3.6 28.3 1.0
CA A:CYS130 3.9 29.0 1.0
CD A:GLN76 4.1 27.6 1.0
C26 A:SB8501 4.1 39.5 0.5
OE1 A:GLN76 4.2 21.2 1.0
ND1 A:HIS177 4.3 20.2 1.0
CG A:HIS173 4.3 24.2 1.0
CG A:HIS177 4.3 16.1 1.0
ND1 A:HIS173 4.3 28.6 1.0
N A:LEU131 4.3 28.4 1.0
C26 A:SB8501 4.4 37.3 0.5
O24 A:SB8501 4.4 41.7 0.5
C25 A:SB8501 4.5 43.6 0.5
O24 A:SB8501 4.5 48.1 0.5
OE1 A:GLU174 4.6 20.7 1.0
C A:CYS130 4.6 32.7 1.0
O A:HOH3009 4.6 22.9 1.0
OE2 A:GLU174 4.7 24.6 1.0
O A:GLY129 4.7 32.1 1.0
C25 A:SB8501 4.8 39.5 0.5

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: Wed Oct 9 16:37:09 2024

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