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Copper in PDB 2ztj: Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Alpha-Ketoglutarate

Enzymatic activity of Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Alpha-Ketoglutarate

All present enzymatic activity of Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Alpha-Ketoglutarate:
2.3.3.14;

Protein crystallography data

The structure of Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Alpha-Ketoglutarate, PDB code: 2ztj was solved by T.Okada, T.Tomita, T.Kuzuyama, M.Nishiyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.66 / 1.80
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 135.645, 135.645, 127.102, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 22.4

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Alpha-Ketoglutarate (pdb code 2ztj). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Alpha-Ketoglutarate, PDB code: 2ztj:

Copper binding site 1 out of 1 in 2ztj

Go back to Copper Binding Sites List in 2ztj
Copper binding site 1 out of 1 in the Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Alpha-Ketoglutarate


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Alpha-Ketoglutarate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu384

b:12.4
occ:0.75
 O5 A:AKG383 2.1 20.0 1.0
NE2 A:HIS197 2.1 17.5 1.0
OE1 A:GLU13 2.2 14.2 1.0
NE2 A:HIS195 2.2 12.6 1.0
O1 A:AKG383 2.3 19.8 1.0
O A:HOH428 2.3 14.5 1.0
C2 A:AKG383 2.8 21.5 1.0
C1 A:AKG383 2.9 19.7 1.0
CE1 A:HIS195 3.1 14.7 1.0
CD2 A:HIS197 3.1 12.6 1.0
CD A:GLU13 3.1 14.7 1.0
CE1 A:HIS197 3.1 14.1 1.0
CD2 A:HIS195 3.2 14.5 1.0
OE2 A:GLU13 3.4 15.2 1.0
O A:HOH450 3.9 16.7 1.0
O2 A:AKG383 4.2 22.6 1.0
ND1 A:HIS195 4.2 14.1 1.0
CG2 A:ILE231 4.2 12.5 1.0
NH2 A:ARG12 4.2 13.5 1.0
C3 A:AKG383 4.2 18.0 1.0
ND1 A:HIS197 4.2 16.1 1.0
CG A:HIS197 4.2 13.9 1.0
O A:HOH468 4.3 31.2 1.0
NH1 A:ARG12 4.3 12.9 1.0
CG A:HIS195 4.3 14.4 1.0
CG A:GLU13 4.4 13.3 1.0
C4 A:AKG383 4.5 18.8 1.0
CZ A:ARG12 4.8 13.8 1.0
CB A:GLU13 5.0 13.6 1.0

Reference:

T.Okada, T.Tomita, A.P.Wulandari, T.Kuzuyama, M.Nishiyama. Mechanism of Substrate Recognition and Insight Into Feedback Inhibition of Homocitrate Synthase From Thermus Thermophilus J.Biol.Chem. V. 285 4195 2010.
ISSN: ISSN 0021-9258
PubMed: 19996101
DOI: 10.1074/JBC.M109.086330
Page generated: Wed Jul 31 00:30:26 2024

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