MolNFT v2 · #148078 · protein

CRYSTAL STRUCTURE OF HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1 (IDO1) in complex with ferric heme and an Epacadostat analog

6E41: “CRYSTAL STRUCTURE OF HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1 (IDO1) in complex with ferric heme and an…”. X-ray diffraction at 2.291, 2 ligands (HQS, HEM). MolNFT v2 #148078 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6E41
Type: protein
Length: 1,507 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.291
Source: Homo sapiens
UniProt: P14902
Ligands: HQS, HEM

Structure

x-ray diffraction · resolution 2.291 · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	377	—	P14902
B, C	—	protein	376	—	P14902
D	—	protein	378	—	P14902

Ligands and binding sites

HQS · N-(3-bromo-4-fluorophenyl)-N'-hydroxy-4-{[2-(sulfamoylamino)ethyl]sulfanyl}-1,2,5-oxadiazole-3-carboximidamide · ligand · 6 copies · chains A, B, C, D
HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6E41 · Crystal structure of human indoleamine 2,3-dioxygenase 1 (IDO1) in complex with ferric… · the same entry in another collection · chain A against A, TM-score 1.00
P14902 · AlphaFold monomer V2.0 prediction for indoleamine 2,3-dioxygenase 1 (P14902) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P14902
Elsewhere: RCSB PDB 6E41 · PDBe 6E41 · UniProt P14902

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