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Crystal structure of rat heme oxygenase-1 in complex with biliverdin ixalpha-iron cluster

Analyse Crystal structure of rat heme oxygenase-1 in complex with biliverdin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1J2C
Type
protein
Length
216 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heme oxygenase-1
EC
1.14.99.3
UniProt
P06762
Ligands
BLA, FE
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeme oxygenase-1 (EC 1.14.99.3)protein21673% helix, 0% strandP06762

Ligands and binding sites

  • BLA · Biliverdine IX alpha · ligand · chains A
  • FE · Fe (III) ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13260.730.8536FE, BLA

Compared structures

  • 1J2C · Crystal structure of rat heme oxygenase-1 in complex with biliverdin IXalpha-iron cluster · the same entry in another collection · chain A against A, TM-score 1.00
  • P06762 · AlphaFold monomer V2.0 prediction for heme oxygenase 1 (P06762) · a predicted model of the same protein · chain A against A, TM-score 0.99

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