Atomistry » Iron » PDB 6u97-6uw2 » 6ubp
Atomistry »
  Iron »
    PDB 6u97-6uw2 »
      6ubp »

Iron in PDB 6ubp: Crystal Structure of A Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan

Enzymatic activity of Crystal Structure of A Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan

All present enzymatic activity of Crystal Structure of A Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan:
1.13.11.52;

Protein crystallography data

The structure of Crystal Structure of A Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan, PDB code: 6ubp was solved by K.N.Pham, S.R.Yeh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.34 / 2.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 86.944, 97.727, 130.628, 90, 90, 90
R / Rfree (%) 21.5 / 26.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan (pdb code 6ubp). 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 Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan, PDB code: 6ubp:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 6ubp

Go back to Iron Binding Sites List in 6ubp
Iron binding site 1 out of 2 in the Crystal Structure of A Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan


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 Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:98.2
occ:1.00
 FE A:HEM501 0.0 98.2 1.0
ND A:HEM501 1.9 99.3 1.0
NA A:HEM501 2.0 98.6 1.0
NC A:HEM501 2.1 98.9 1.0
NB A:HEM501 2.1 98.9 1.0
NE2 A:HIS346 2.2 81.1 1.0
C4D A:HEM501 2.9 99.1 1.0
C1D A:HEM501 2.9 99.2 1.0
C1A A:HEM501 3.0 99.1 1.0
C4A A:HEM501 3.0 98.8 1.0
C4C A:HEM501 3.1 98.6 1.0
C1B A:HEM501 3.1 99.0 1.0
CE1 A:HIS346 3.1 81.6 1.0
C4B A:HEM501 3.1 98.6 1.0
C1C A:HEM501 3.1 99.2 1.0
CD2 A:HIS346 3.2 81.8 1.0
CHA A:HEM501 3.3 99.1 1.0
CHD A:HEM501 3.4 98.9 1.0
CHB A:HEM501 3.5 99.2 1.0
CHC A:HEM501 3.5 99.0 1.0
CB A:ALA264 3.9 107.7 1.0
C2D A:HEM501 4.1 99.0 1.0
C3D A:HEM501 4.1 98.5 1.0
C2A A:HEM501 4.2 99.2 1.0
C3A A:HEM501 4.2 98.5 1.0
ND1 A:HIS346 4.2 81.8 1.0
C3C A:HEM501 4.3 98.8 1.0
C2C A:HEM501 4.3 98.9 1.0
CG A:HIS346 4.3 82.6 1.0
C2B A:HEM501 4.3 98.7 1.0
C3B A:HEM501 4.4 98.2 1.0
CA A:ALA264 4.8 107.7 1.0
C A:ALA264 4.8 106.5 1.0
N A:GLY265 4.9 105.0 1.0

Iron binding site 2 out of 2 in 6ubp

Go back to Iron Binding Sites List in 6ubp
Iron binding site 2 out of 2 in the Crystal Structure of A Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan


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 Photochemical Intermediate of Human Indoleamine 2,3-Dioxygenase 1 in Complex with Carbon Monoxide and Tryptophan within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:96.3
occ:1.00
 FE B:HEM501 0.0 96.3 1.0
ND B:HEM501 1.9 97.1 1.0
NA B:HEM501 2.0 98.1 1.0
NC B:HEM501 2.1 95.5 1.0
NB B:HEM501 2.1 96.5 1.0
NE2 B:HIS346 2.3 103.2 1.0
C1D B:HEM501 2.9 96.2 1.0
C4D B:HEM501 2.9 97.1 1.0
C1A B:HEM501 3.0 99.1 1.0
C4A B:HEM501 3.0 98.7 1.0
C4C B:HEM501 3.0 95.2 1.0
C1B B:HEM501 3.1 97.1 1.0
C4B B:HEM501 3.1 96.0 1.0
CE1 B:HIS346 3.1 103.1 1.0
C1C B:HEM501 3.1 94.9 1.0
CD2 B:HIS346 3.3 103.3 1.0
CHA B:HEM501 3.3 97.8 1.0
CHD B:HEM501 3.3 95.7 1.0
CHB B:HEM501 3.4 97.6 1.0
CHC B:HEM501 3.5 95.1 1.0
CB B:ALA264 3.9 117.0 1.0
C3D B:HEM501 4.1 97.1 1.0
C2D B:HEM501 4.1 96.3 1.0
O B:HOH607 4.2 138.0 1.0
C2A B:HEM501 4.2 100.9 1.0
C3A B:HEM501 4.2 100.1 1.0
C3C B:HEM501 4.3 95.3 1.0
ND1 B:HIS346 4.3 103.2 1.0
C2C B:HEM501 4.3 94.8 1.0
C2B B:HEM501 4.3 96.7 1.0
C3B B:HEM501 4.4 96.2 1.0
CG B:HIS346 4.4 103.9 1.0
C B:ALA264 4.7 114.5 1.0
N B:GLY265 4.8 112.9 1.0
CA B:ALA264 4.8 116.3 1.0

Reference:

K.N.Pham, A.Lewis-Ballester, S.R.Yeh. Conformational Plasticity in Human Heme-Based Dioxygenases. J.Am.Chem.Soc. 2020.
ISSN: ESSN 1520-5126
PubMed: 33373218
DOI: 10.1021/JACS.0C09970
Page generated: Wed Aug 7 12:16:53 2024

Last articles

Ca in 5TR2
Ca in 5TRQ
Ca in 5TRX
Ca in 5TQG
Ca in 5TQF
Ca in 5TQE
Ca in 5TNC
Ca in 5TP9
Ca in 5TP0
Ca in 5TMN
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy