Structure of PDB 3moo Chain A Binding Site BS02

Receptor Information

>3moo Chain A (length=207) Species: 1717 (Corynebacterium diphtheriae)

GLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFYTAL
EQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITASPAV
IDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGVDPE
ALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVFNHQ
VFADLGK

Ligand information

• Ligand ID: AZI
• InChI: InChI=1S/N3/c1-3-2/q-1
• InChIKey: IVRMZWNICZWHMI-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [N-]=[N+]=[N-]
• Formula: N3
• Name: AZIDE ION
• ChEMBL: CHEMBL79455
• PDB chain: 3moo Chain A Residue 217

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3moo Enzymatic ring-opening mechanism of verdoheme by the heme oxygenase: a combined X-ray crystallography and QM/MM study.
• Resolution: 1.71 Å
• Binding residue (original residue number in PDB): G135 G139 G140
• Binding residue (residue number reindexed from 1): G129 G133 G134
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H25 Y53 V131 R132 G135 D136 G140
• Catalytic site (residue number reindexed from 1): H19 Y47 V125 R126 G129 D130 G134
• Enzyme Commision number: 1.14.14.18: heme oxygenase (biliverdin-producing).

Gene Ontology

Molecular Function

• GO:0004392 heme oxygenase (decyclizing) activity
• GO:0016491 oxidoreductase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006788 heme oxidation
• GO:0006979 response to oxidative stress
• GO:0042167 heme catabolic process

External links

• PDB: RCSB:3moo, PDBe:3moo, PDBj:3moo
• PDBsum: 3moo
• PubMed: 20806922
• UniProt: Q54AI1