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Zinc in PDB 1l0h: Crystal Structure of Butyryl-Acp From E.Coli

Protein crystallography data

The structure of Crystal Structure of Butyryl-Acp From E.Coli, PDB code: 1l0h 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) 10.00 / 2.00
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 63.360, 63.360, 37.049, 90.00, 90.00, 120.00
R / Rfree (%) 20.5 / 25.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Butyryl-Acp From E.Coli (pdb code 1l0h). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Butyryl-Acp From E.Coli, PDB code: 1l0h:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1l0h

Go back to Zinc Binding Sites List in 1l0h
Zinc binding site 1 out of 2 in the Crystal Structure of Butyryl-Acp From E.Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Butyryl-Acp From E.Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn80

b:48.8
occ:1.00
OE2 A:GLU4 2.2 33.0 1.0
O A:HOH131 2.2 48.9 1.0
OE1 A:GLU4 2.8 39.1 1.0
CD A:GLU4 2.8 35.5 1.0
CB A:THR2 4.0 37.8 1.0
N A:ILE3 4.1 35.2 1.0
ND2 A:ASN73 4.2 22.8 1.0
CG2 A:THR2 4.3 37.4 1.0
CG A:GLU4 4.3 32.4 1.0
CB A:ILE3 4.4 37.4 1.0
N A:GLU4 4.5 28.4 1.0
CA A:THR2 4.8 42.1 1.0
CA A:ILE3 4.8 33.1 1.0
OD1 A:ASN73 4.8 31.5 1.0
CG1 A:ILE3 4.9 40.3 1.0
OG1 A:THR2 4.9 37.5 1.0
CG A:ASN73 5.0 26.4 1.0
C A:THR2 5.0 39.7 1.0
CB A:GLU4 5.0 29.6 1.0

Zinc binding site 2 out of 2 in 1l0h

Go back to Zinc Binding Sites List in 1l0h
Zinc binding site 2 out of 2 in the Crystal Structure of Butyryl-Acp From E.Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Butyryl-Acp From E.Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn81

b:29.2
occ:1.00
OD1 A:ASP31 2.0 25.9 1.0
O A:HOH92 2.1 30.9 1.0
CG A:ASP31 2.7 28.0 1.0
OD2 A:ASP31 2.8 27.5 1.0
O A:HOH84 3.6 44.6 1.0
CB A:ASP31 4.2 21.3 1.0
CB A:GLU30 4.2 39.5 1.0
N A:ASP31 4.5 22.6 1.0
CA A:ASP31 4.7 20.4 1.0
C A:GLU30 4.8 23.8 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: Sun Oct 13 04:44:06 2024

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