Atomistry » Zinc » PDB 2a25-2aer » 2ac2
Atomistry »
  Zinc »
    PDB 2a25-2aer »
      2ac2 »

Zinc in PDB 2ac2: Crystal Structure of the TYR13PHE Mutant Variant of Bacillus Subtilis Ferrochelatase with Zn(2+) Bound at the Active Site

Enzymatic activity of Crystal Structure of the TYR13PHE Mutant Variant of Bacillus Subtilis Ferrochelatase with Zn(2+) Bound at the Active Site

All present enzymatic activity of Crystal Structure of the TYR13PHE Mutant Variant of Bacillus Subtilis Ferrochelatase with Zn(2+) Bound at the Active Site:
4.99.1.1;

Protein crystallography data

The structure of Crystal Structure of the TYR13PHE Mutant Variant of Bacillus Subtilis Ferrochelatase with Zn(2+) Bound at the Active Site, PDB code: 2ac2 was solved by S.Shipovskov, T.Karlberg, M.Fodje, M.D.Hansson, G.C.Ferreira, M.Hansson, C.T.Reimann, S.Al-Karadaghi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.170, 49.700, 117.970, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 25.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the TYR13PHE Mutant Variant of Bacillus Subtilis Ferrochelatase with Zn(2+) Bound at the Active Site (pdb code 2ac2). 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 the TYR13PHE Mutant Variant of Bacillus Subtilis Ferrochelatase with Zn(2+) Bound at the Active Site, PDB code: 2ac2:

Zinc binding site 1 out of 1 in 2ac2

Go back to Zinc Binding Sites List in 2ac2
Zinc binding site 1 out of 1 in the Crystal Structure of the TYR13PHE Mutant Variant of Bacillus Subtilis Ferrochelatase with Zn(2+) Bound at the Active Site


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 the TYR13PHE Mutant Variant of Bacillus Subtilis Ferrochelatase with Zn(2+) Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:52.9
occ:0.93
 NE2 A:HIS183 2.4 22.2 1.0
CE1 A:HIS183 3.1 22.6 1.0
OE2 A:GLU264 3.4 32.7 1.0
CD2 A:HIS183 3.5 23.0 1.0
O A:SER222 3.5 26.4 1.0
OE1 A:GLU264 3.7 35.7 1.0
CD A:GLU264 4.0 32.8 1.0
ND1 A:HIS183 4.4 23.4 1.0
CB A:SER222 4.4 26.5 1.0
CG A:HIS183 4.5 22.0 1.0
CZ A:PHE13 4.6 27.0 1.0
C A:SER222 4.7 26.0 1.0
CE2 A:PHE13 4.7 27.9 1.0
O A:HOH518 4.9 15.2 1.0
O A:HOH532 5.0 21.7 1.0

Reference:

S.Shipovskov, T.Karlberg, M.Fodje, M.D.Hansson, G.C.Ferreira, M.Hansson, C.T.Reimann, S.Al-Karadaghi. Metallation of the Transition-State Inhibitor N-Methyl Mesoporphyrin By Ferrochelatase: Implications For the Catalytic Reaction Mechanism. J.Mol.Biol. V. 352 1081 2005.
ISSN: ISSN 0022-2836
PubMed: 16140324
DOI: 10.1016/J.JMB.2005.08.002
Page generated: Wed Oct 16 21:35:54 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy