Structure of PDB 2hk6 Chain A Binding Site BS01

Receptor Information
>2hk6 Chain A (length=309) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SRKKMGLLVMAYGTPYKEEDIERYYTHIRRGRKPEPEMLQDLKDRYEAIG
GISPLAQITEQQAHNLEQHLNEIQDEITFKAYIGLKHIEPFIEDAVAEMH
KDGITEAVSIVLAPHFSTFSVQSYNKRAKEEAEKLGGLTITSVESWYDEP
KFVTYWVDRVKETYASMPEDERENAMLIVSAHSLPEKIKEFGDPYPDQLH
ESAKLIAEGAGVSEYAVGWQSEGNTPDPWLGPDVQDLTRDLFEQKGYQAF
VYVPVGFVADHLEVLYDNDYECKVVTDDIGASYYRPEMPNAKPEFIDALA
TVVLKKLGR
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain2hk6 Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2hk6 Amino Acid Residues His183 and Glu264 in Bacillus subtilis Ferrochelatase Direct and Facilitate the Insertion of Metal Ion into Protoporphyrin IX
Resolution1.71 Å
Binding residue
(original residue number in PDB)		H183 E264
Binding residue
(residue number reindexed from 1)		H182 E263
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y13 I29 P35 K87 H88 H183 D261 E264 D268
Catalytic site (residue number reindexed from 1) Y12 I28 P34 K86 H87 H182 D260 E263 D267
Enzyme Commision number 4.99.1.9: coproporphyrin ferrochelatase.
Gene Ontology
Molecular Function
GO:0004325 ferrochelatase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006783 heme biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2hk6, PDBe:2hk6, PDBj:2hk6
PDBsum2hk6
PubMed17198378
UniProtP32396|CPFC_BACSU Coproporphyrin III ferrochelatase (Gene Name=cpfC)

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