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Chlorine in PDB 2go4: Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Tu-514

Protein crystallography data

The structure of Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Tu-514, PDB code: 2go4 was solved by H.A.Gennadios, D.A.Whittington, X.Li, C.A.Fierke, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.70
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 100.729, 100.729, 121.299, 90.00, 90.00, 120.00
R / Rfree (%) 21 / 24.1

Other elements in 2go4:

The structure of Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Tu-514 also contains other interesting chemical elements:

Zinc (Zn) 5 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Tu-514 (pdb code 2go4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Tu-514, PDB code: 2go4:

Chlorine binding site 1 out of 1 in 2go4

Go back to Chlorine Binding Sites List in 2go4
Chlorine binding site 1 out of 1 in the Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Tu-514


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Tu-514 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:55.1
occ:1.00
ZN A:ZN604 2.0 51.7 0.8
NE2 A:HIS58 3.1 56.2 1.0
NE2 A:HIS200 3.2 63.0 1.0
O A:HOH925 3.7 36.8 1.0
CE1 A:HIS58 3.7 56.9 1.0
CE1 A:HIS200 3.9 62.8 1.0
CD2 A:HIS58 4.1 55.0 1.0
CD2 A:HIS200 4.2 62.3 1.0
ND1 A:HIS58 4.8 56.1 1.0
CB A:ASN57 4.9 60.9 1.0
OD1 A:ASN57 4.9 66.7 1.0

Reference:

H.A.Gennadios, D.A.Whittington, X.Li, C.A.Fierke, D.W.Christianson. Mechanistic Inferences From the Binding of Ligands to Lpxc, A Metal-Dependent Deacetylase Biochemistry V. 45 7940 2006.
ISSN: ISSN 0006-2960
PubMed: 16800620
DOI: 10.1021/BI060823M
Page generated: Sat Dec 12 09:06:35 2020

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