Structure of PDB 1c1h Chain A

Receptor sequence
>1c1hA (length=306) Species: 1423 (Bacillus subtilis) [Search protein sequence]
KMGLLVMAYGTPYKEEDIERYYTHIRRGRKPEPEMLQDLKDRYEAIGGIS
PLAQITEQQAHNLEQHLNEIQDEITFKAYIGLKHIEPFIEDAVAEMHKDG
ITEAVSIVLAPHFSTFSVQSYNKRAKEEAEKLGGLTITSVESWYDEPKFV
TYWVDRVKETYASMPEDERENAMLIVSAHSLPEKIKEFGDPYPDQLHESA
KLIAEGAGVSEYAVGWQSEGNTPDPWLGPDVQDLTRDLFEQKGYQAFVYV
PVGFVADHLEVLYDNDYECKVVTDDIGASYYRPEMPNAKPEFIDALATVV
LKKLGR
3D structure
PDB1c1h Structural and mechanistic basis of porphyrin metallation by ferrochelatase.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) Y9 I25 P31 K83 H84 H179 D257 E260 D264
Enzyme Commision number 4.99.1.9: coproporphyrin ferrochelatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MMP A Y13 I29 R30 F120 H183 K188 W230 Y9 I25 R26 F116 H179 K184 W226
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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Cellular Component
External links
PDB RCSB:1c1h, PDBe:1c1h, PDBj:1c1h
PDBsum1c1h
PubMed10704318
UniProtP32396|CPFC_BACSU Coproporphyrin III ferrochelatase (Gene Name=cpfC)

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