Atomistry » Copper » PDB 2z7y-3aws » 2ztk
Atomistry »
  Copper »
    PDB 2z7y-3aws »
      2ztk »

Copper in PDB 2ztk: Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Homocitrate

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

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

Protein crystallography data

The structure of Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Homocitrate, PDB code: 2ztk 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) 44.36 / 1.96
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 135.508, 135.508, 127.062, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 22.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Homocitrate Synthase From Thermus Thermophilus Complexed with Homocitrate (pdb code 2ztk). 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 Homocitrate, PDB code: 2ztk:

Copper binding site 1 out of 1 in 2ztk

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


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 Homocitrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu384

b:14.2
occ:0.75
O7 A:HCA383 2.0 22.4 1.0
NE2 A:HIS197 2.1 17.7 1.0
NE2 A:HIS195 2.2 19.4 1.0
OE1 A:GLU13 2.2 17.6 1.0
O A:HOH547 2.3 16.0 1.0
O5 A:HCA383 2.3 23.1 1.0
C7 A:HCA383 3.0 24.5 1.0
CD2 A:HIS197 3.0 16.9 1.0
C3 A:HCA383 3.0 25.2 1.0
CE1 A:HIS195 3.1 18.2 1.0
CE1 A:HIS197 3.1 16.9 1.0
CD A:GLU13 3.2 17.6 1.0
CD2 A:HIS195 3.2 18.5 1.0
OE2 A:GLU13 3.5 18.9 1.0
O A:HOH418 3.9 20.1 1.0
C2 A:HCA383 4.1 29.3 1.0
CG A:HIS197 4.2 16.5 1.0
C1 A:HCA383 4.2 37.3 1.0
ND1 A:HIS197 4.2 17.9 1.0
O6 A:HCA383 4.2 25.1 1.0
C4 A:HCA383 4.2 21.0 1.0
CG2 A:ILE231 4.2 13.6 1.0
O1 A:HCA383 4.2 37.6 1.0
ND1 A:HIS195 4.2 18.1 1.0
NH2 A:ARG12 4.3 18.4 1.0
NH1 A:ARG12 4.3 16.0 1.0
CG A:HIS195 4.3 18.0 1.0
C5 A:HCA383 4.4 20.4 1.0
CG A:GLU13 4.5 17.9 1.0
CZ A:ARG12 4.8 19.7 1.0
O2 A:HCA383 4.9 39.8 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: Sun Dec 13 11:08:32 2020

Last articles

Zn in 7L3L
Zn in 7KSO
Zn in 7KSR
Zn in 7KTP
Zn in 7LMM
Zn in 7LMK
Zn in 7LLZ
Zn in 7LLF
Zn in 7L0N
Zn in 7LBR
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy