Iron in PDB 6sv3: Structure of Coproheme-Lmcpfc

Enzymatic activity of Structure of Coproheme-Lmcpfc

All present enzymatic activity of Structure of Coproheme-Lmcpfc:
4.99.1.1;

Protein crystallography data

The structure of Structure of Coproheme-Lmcpfc, PDB code: 6sv3 was solved by S.Hofbauer, J.Helm, K.Djinovic-Carugo, P.G.Furtmueller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.50 / 1.64
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.470, 68.140, 62.910, 90.00, 103.06, 90.00
R / Rfree (%) 17.1 / 20.1

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Coproheme-Lmcpfc (pdb code 6sv3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of Coproheme-Lmcpfc, PDB code: 6sv3:

Iron binding site 1 out of 1 in 6sv3

Go back to Iron Binding Sites List in 6sv3
Iron binding site 1 out of 1 in the Structure of Coproheme-Lmcpfc


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Coproheme-Lmcpfc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:26.1
occ:1.00
FE A:FEC401 0.0 26.1 1.0
ND A:FEC401 2.0 19.8 1.0
NC A:FEC401 2.0 24.9 1.0
NA A:FEC401 2.0 20.5 1.0
NB A:FEC401 2.0 24.7 1.0
OH A:TYR12 2.7 36.0 1.0
CZ A:TYR12 3.0 31.9 1.0
C1A A:FEC401 3.0 21.5 1.0
C4D A:FEC401 3.0 20.1 1.0
C1C A:FEC401 3.0 27.6 1.0
C4B A:FEC401 3.0 29.7 1.0
C1D A:FEC401 3.1 18.4 1.0
C4C A:FEC401 3.1 27.3 1.0
C1B A:FEC401 3.1 18.4 1.0
C4A A:FEC401 3.1 28.6 1.0
NE2 A:HIS182 3.2 17.8 1.0
CHC A:FEC401 3.4 31.3 1.0
CHA A:FEC401 3.4 22.7 1.0
CHB A:FEC401 3.4 24.8 1.0
CE1 A:TYR12 3.4 26.3 1.0
CHD A:FEC401 3.4 27.2 1.0
CD2 A:HIS182 3.7 18.4 1.0
CE2 A:TYR12 3.7 23.2 1.0
OE1 A:GLU263 3.7 25.4 0.4
OE1 A:GLU263 3.9 22.5 0.6
CE1 A:HIS182 4.1 18.0 1.0
C2A A:FEC401 4.3 22.9 1.0
C3D A:FEC401 4.3 19.3 1.0
C2C A:FEC401 4.3 33.5 1.0
C2D A:FEC401 4.3 21.9 1.0
C3A A:FEC401 4.3 27.6 1.0
C3C A:FEC401 4.3 30.4 1.0
C3B A:FEC401 4.3 26.5 1.0
C2B A:FEC401 4.3 21.7 1.0
O A:HOH554 4.3 27.5 1.0
CD1 A:TYR12 4.4 26.2 1.0
O A:HOH548 4.6 36.0 1.0
CD2 A:TYR12 4.6 23.6 1.0
CD A:GLU263 4.7 25.3 0.6
CG A:HIS182 4.7 18.3 1.0
CD A:GLU263 4.8 23.5 0.4
CG A:TYR12 4.9 23.8 1.0
ND1 A:HIS182 4.9 19.1 1.0

Reference:

S.Hofbauer, J.Helm, C.Obinger, K.Djinovic-Carugo, P.G.Furtmuller. Crystal Structures and Calorimetry Reveal Catalytically Relevant Binding Mode of Coproporphyrin and Coproheme in Coproporphyrin Ferrochelatase. Febs J. 2019.
ISSN: ISSN 1742-464X
PubMed: 31794133
DOI: 10.1111/FEBS.15164
Page generated: Sun Dec 13 17:06:16 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy