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Arsenic in PDB 1l0i: Crystal Structure of Butyryl-Acp I62M Mutant

Protein crystallography data

The structure of Crystal Structure of Butyryl-Acp I62M Mutant, PDB code: 1l0i was solved by A.Roujeinikova, C.Baldock, W.J.Simon, J.Gilroy, P.J.Baker, A.R.Stuitje, D.W.Rice, A.R.Slabas, J.B.Rafferty, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 1.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 27.347, 41.941, 64.533, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 19.3

Other elements in 1l0i:

The structure of Crystal Structure of Butyryl-Acp I62M Mutant also contains other interesting chemical elements:

Zinc (Zn) 7 atoms
Sodium (Na) 1 atom

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Butyryl-Acp I62M Mutant (pdb code 1l0i). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of Butyryl-Acp I62M Mutant, PDB code: 1l0i:

Arsenic binding site 1 out of 1 in 1l0i

Go back to Arsenic Binding Sites List in 1l0i
Arsenic binding site 1 out of 1 in the Crystal Structure of Butyryl-Acp I62M Mutant


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Butyryl-Acp I62M Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1003

b:27.6
occ:0.70
AS A:CAC1003 0.0 27.6 0.7
O1 A:CAC1003 1.7 35.1 0.7
O2 A:CAC1003 1.8 24.4 0.7
C2 A:CAC1003 2.0 74.8 0.7
C1 A:CAC1003 2.0 42.6 0.7
ZN A:ZN1002 3.2 13.2 0.5
O A:HOH2195 4.3 34.6 1.0
OE2 A:GLU13 4.5 19.5 1.0
O A:HOH2319 4.5 29.1 1.0
OE1 A:GLU13 4.7 25.9 1.0
CD A:GLU13 4.9 17.7 1.0
O A:HOH2078 5.0 30.2 1.0

Reference:

A.Roujeinikova, C.Baldock, W.J.Simon, J.Gilroy, P.J.Baker, A.R.Stuitje, D.W.Rice, A.R.Slabas, J.B.Rafferty. X-Ray Crystallographic Studies on Butyryl-Acp Reveal Flexibility of the Structure Around A Putative Acyl Chain Binding Site Structure V. 10 825 2002.
ISSN: ISSN 0969-2126
PubMed: 12057197
DOI: 10.1016/S0969-2126(02)00775-X
Page generated: Sat Dec 12 01:36:47 2020

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