Atomistry » Iron » PDB 1eb7-1esz » 1ep1
Atomistry »
  Iron »
    PDB 1eb7-1esz »
      1ep1 »

Iron in PDB 1ep1: Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B

Enzymatic activity of Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B

All present enzymatic activity of Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B:
1.3.3.1;

Protein crystallography data

The structure of Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B, PDB code: 1ep1 was solved by P.Rowland, S.Norager, K.F.Jensen, S.Larsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.70 / 2.20
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 202.670, 202.670, 81.110, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 25.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B (pdb code 1ep1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B, PDB code: 1ep1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1ep1

Go back to Iron Binding Sites List in 1ep1
Iron binding site 1 out of 2 in the Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe503

b:32.0
occ:1.00
FE1 B:FES503 0.0 32.0 1.0
S2 B:FES503 2.2 32.4 1.0
SG B:CYS231 2.2 33.4 1.0
S1 B:FES503 2.3 31.5 1.0
SG B:CYS226 2.3 27.4 1.0
FE2 B:FES503 2.7 32.2 1.0
CB B:CYS231 3.4 31.1 1.0
CB B:CYS226 3.4 25.5 1.0
N B:CYS226 3.5 27.2 1.0
N B:CYS231 3.6 33.0 1.0
N B:GLY227 3.6 32.6 1.0
N B:TYR232 3.8 36.9 1.0
CA B:CYS231 3.8 33.0 1.0
CA B:CYS226 3.9 28.4 1.0
N B:ALA233 4.2 37.2 1.0
C B:CYS231 4.2 35.9 1.0
C B:CYS226 4.2 30.1 1.0
SG B:CYS249 4.2 34.3 1.0
N B:GLY229 4.3 29.3 1.0
N B:ALA230 4.4 29.0 1.0
CB B:ALA233 4.4 36.7 1.0
N B:ALA225 4.5 25.7 1.0
CA B:GLY227 4.6 34.0 1.0
C B:ALA225 4.6 24.9 1.0
N B:ILE228 4.6 31.7 1.0
SG B:CYS234 4.6 32.0 1.0
CA B:GLY229 4.7 27.6 1.0
C B:GLY229 4.7 27.6 1.0
C B:ALA230 4.7 31.5 1.0
CA B:TYR232 4.8 37.5 1.0
CB B:ALA225 4.8 25.4 1.0
CA B:ALA225 4.9 25.9 1.0
CA B:ALA233 4.9 37.4 1.0
C B:GLY227 5.0 35.2 1.0

Iron binding site 2 out of 2 in 1ep1

Go back to Iron Binding Sites List in 1ep1
Iron binding site 2 out of 2 in the Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe503

b:32.2
occ:1.00
FE2 B:FES503 0.0 32.2 1.0
SG B:CYS249 2.2 34.3 1.0
SG B:CYS234 2.2 32.0 1.0
S1 B:FES503 2.2 31.5 1.0
S2 B:FES503 2.3 32.4 1.0
FE1 B:FES503 2.7 32.0 1.0
CB B:CYS249 3.3 36.0 1.0
CB B:CYS234 3.4 35.7 1.0
N B:CYS234 4.1 38.5 1.0
N B:GLY229 4.3 29.3 1.0
N B:CYS249 4.3 36.7 1.0
SG B:CYS226 4.4 27.4 1.0
CA B:CYS234 4.4 38.2 1.0
N B:GLY227 4.4 32.6 1.0
CA B:CYS249 4.5 36.1 1.0
SG B:CYS231 4.5 33.4 1.0
CA B:GLY229 4.5 27.6 1.0
CA B:GLY227 4.6 34.0 1.0
N B:ALA233 4.6 37.2 1.0
CB B:LYS247 4.7 38.5 1.0
N B:TYR232 4.8 36.9 1.0
C B:GLY227 4.8 35.2 1.0
N B:ILE228 4.9 31.7 1.0

Reference:

P.Rowland, S.Norager, K.F.Jensen, S.Larsen. Structure of Dihydroorotate Dehydrogenase B: Electron Transfer Between Two Flavin Groups Bridged By An Iron-Sulphur Cluster. Structure Fold.Des. V. 8 1227 2000.
ISSN: ISSN 0969-2126
PubMed: 11188687
DOI: 10.1016/S0969-2126(00)00530-X
Page generated: Sat Aug 3 04:35:18 2024

Last articles

As in 2VQH
As in 2VDL
As in 2VEQ
As in 2VDK
As in 2V5C
As in 2V96
As in 2RA8
As in 2PQ3
As in 2OUI
As in 2RL7
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy