Atomistry » Zinc » PDB 2paj-2poj » 2pkp
Atomistry »
  Zinc »
    PDB 2paj-2poj »
      2pkp »

Zinc in PDB 2pkp: Crystal Structure of 3-Isopropylmalate Dehydratase (Leud) From Methhanocaldococcus Jannaschii DSM2661 (MJ1271)

Enzymatic activity of Crystal Structure of 3-Isopropylmalate Dehydratase (Leud) From Methhanocaldococcus Jannaschii DSM2661 (MJ1271)

All present enzymatic activity of Crystal Structure of 3-Isopropylmalate Dehydratase (Leud) From Methhanocaldococcus Jannaschii DSM2661 (MJ1271):
4.2.1.114;

Protein crystallography data

The structure of Crystal Structure of 3-Isopropylmalate Dehydratase (Leud) From Methhanocaldococcus Jannaschii DSM2661 (MJ1271), PDB code: 2pkp was solved by J.Jeyakanthan, D.R.Gayathri, D.Velmurugan, Y.Agari, A.Ebihara, S.Kuramitsu, A.Shinkai, Y.Shiro, S.Yokoyama, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.12 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 90.992, 108.283, 45.449, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 24.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of 3-Isopropylmalate Dehydratase (Leud) From Methhanocaldococcus Jannaschii DSM2661 (MJ1271) (pdb code 2pkp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of 3-Isopropylmalate Dehydratase (Leud) From Methhanocaldococcus Jannaschii DSM2661 (MJ1271), PDB code: 2pkp:

Zinc binding site 1 out of 1 in 2pkp

Go back to Zinc Binding Sites List in 2pkp
Zinc binding site 1 out of 1 in the Crystal Structure of 3-Isopropylmalate Dehydratase (Leud) From Methhanocaldococcus Jannaschii DSM2661 (MJ1271)


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 3-Isopropylmalate Dehydratase (Leud) From Methhanocaldococcus Jannaschii DSM2661 (MJ1271) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn171

b:36.3
occ:1.00
 O A:HOH493 2.0 28.5 1.0
OD1 A:ASP13 2.1 35.6 1.0
SG A:CYS63 2.2 31.7 1.0
OD2 A:ASP13 2.5 33.6 1.0
CG A:ASP13 2.6 31.4 1.0
CB A:CYS63 3.2 31.1 1.0
ND2 A:ASN60 3.6 24.6 1.0
CB A:ASP13 4.1 28.9 1.0
O A:ASP13 4.5 24.5 1.0
CA A:CYS63 4.6 32.9 1.0
CB A:ASP15 4.7 30.3 1.0
CA A:ASP13 4.7 25.6 1.0
C A:CYS63 4.8 39.0 1.0
CG A:ASN60 4.9 23.5 1.0
C A:ASP13 4.9 25.8 1.0
N A:GLY64 5.0 46.4 1.0

Reference:

J.Jeyakanthan, R.M.Drevland, D.R.Gayathri, D.Velmurugan, A.Shinkai, S.Kuramitsu, S.Yokoyama, D.E.Graham. Substrate Specificity Determinants of the Methanogen Homoaconitase Enzyme: Structure and Function of the Small Subunit Biochemistry V. 49 2687 2010.
ISSN: ISSN 0006-2960
PubMed: 20170198
DOI: 10.1021/BI901766Z
Page generated: Thu Oct 17 03:05:36 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy