Atomistry » Iron » PDB 8csq-8djr » 8d8p
Atomistry »
  Iron »
    PDB 8csq-8djr »
      8d8p »

Iron in PDB 8d8p: Crystal Structure of A Novel Fatty Acid Decarboxylase From Rothia Nasimurium

Protein crystallography data

The structure of Crystal Structure of A Novel Fatty Acid Decarboxylase From Rothia Nasimurium, PDB code: 8d8p was solved by P.S.Vieira, M.T.Murakami, L.M.Zanphorlin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.41 / 2.75
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 57.545, 203.38, 316.351, 90, 90, 90
R / Rfree (%) 22.8 / 26.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Novel Fatty Acid Decarboxylase From Rothia Nasimurium (pdb code 8d8p). 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 A Novel Fatty Acid Decarboxylase From Rothia Nasimurium, PDB code: 8d8p:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 8d8p

Go back to Iron Binding Sites List in 8d8p
Iron binding site 1 out of 2 in the Crystal Structure of A Novel Fatty Acid Decarboxylase From Rothia Nasimurium


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 A Novel Fatty Acid Decarboxylase From Rothia Nasimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:68.0
occ:1.00
FE A:HEM501 0.0 68.0 1.0
NA A:HEM501 2.0 68.7 1.0
NB A:HEM501 2.0 67.0 1.0
ND A:HEM501 2.0 70.3 1.0
NC A:HEM501 2.0 69.1 1.0
SG A:CYS378 2.3 73.9 1.0
C1A A:HEM501 3.1 67.7 1.0
C4D A:HEM501 3.1 69.6 1.0
C1B A:HEM501 3.1 65.8 1.0
C4A A:HEM501 3.1 66.9 1.0
C4B A:HEM501 3.1 67.9 1.0
C4C A:HEM501 3.1 68.3 1.0
C1C A:HEM501 3.1 69.0 1.0
C1D A:HEM501 3.1 68.2 1.0
CHA A:HEM501 3.4 67.8 1.0
CHB A:HEM501 3.4 65.0 1.0
CHD A:HEM501 3.4 67.5 1.0
CHC A:HEM501 3.4 68.0 1.0
CB A:CYS378 3.6 67.3 1.0
C2A A:HEM501 4.3 68.2 1.0
C3D A:HEM501 4.3 68.6 1.0
C3A A:HEM501 4.3 67.5 1.0
C3B A:HEM501 4.3 67.9 1.0
C2B A:HEM501 4.3 66.8 1.0
C3C A:HEM501 4.3 67.6 1.0
C2D A:HEM501 4.3 68.6 1.0
C2C A:HEM501 4.3 67.8 1.0
O2 A:PLM502 4.4 72.1 1.0
C2 A:PLM502 4.4 66.0 1.0
CB A:PRO247 4.4 69.0 1.0
CA A:CYS378 4.5 69.2 1.0
OE1 A:GLN367 4.7 68.3 1.0
C1 A:PLM502 4.8 69.0 1.0
CG A:PRO247 4.9 69.0 1.0

Iron binding site 2 out of 2 in 8d8p

Go back to Iron Binding Sites List in 8d8p
Iron binding site 2 out of 2 in the Crystal Structure of A Novel Fatty Acid Decarboxylase From Rothia Nasimurium


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 A Novel Fatty Acid Decarboxylase From Rothia Nasimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:78.8
occ:1.00
FE B:HEM501 0.0 78.8 1.0
NA B:HEM501 2.0 71.7 1.0
NB B:HEM501 2.0 72.5 1.0
NC B:HEM501 2.0 73.3 1.0
ND B:HEM501 2.1 74.4 1.0
SG B:CYS378 2.3 75.4 1.0
C1A B:HEM501 3.0 72.9 1.0
C4A B:HEM501 3.1 71.5 1.0
C1B B:HEM501 3.1 72.0 1.0
C4C B:HEM501 3.1 71.7 1.0
C1C B:HEM501 3.1 73.6 1.0
C1D B:HEM501 3.1 73.8 1.0
C4B B:HEM501 3.1 71.7 1.0
C4D B:HEM501 3.1 72.2 1.0
CB B:CYS378 3.2 74.2 1.0
CHB B:HEM501 3.4 71.5 1.0
CHD B:HEM501 3.4 74.3 1.0
CHA B:HEM501 3.4 71.8 1.0
CHC B:HEM501 3.4 72.7 1.0
CA B:CYS378 4.2 74.4 1.0
C2A B:HEM501 4.3 73.8 1.0
C3A B:HEM501 4.3 72.8 1.0
C2C B:HEM501 4.3 73.2 1.0
C3C B:HEM501 4.3 70.2 1.0
C2B B:HEM501 4.3 71.5 1.0
C3B B:HEM501 4.3 71.5 1.0
C2D B:HEM501 4.3 73.4 1.0
C3D B:HEM501 4.3 71.8 1.0
CB B:PRO247 4.4 70.3 1.0
OE1 B:GLN367 4.4 75.7 1.0
C2 B:PLM502 4.6 68.6 1.0
O B:PRO379 4.8 85.1 1.0
CG B:PRO247 5.0 71.9 1.0

Reference:

P.S.Vieira, M.T.Murakami, L.M.Zanphorlin. Crystal Structure of A Novel Fatty Acid Decarboxylase From Rothia Nasimurium Proc.Natl.Acad.Sci.Usa 2023.
ISSN: ESSN 1091-6490
Page generated: Fri Aug 9 23:22:23 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