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: Wed Jul 31 00:30:27 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy