Structure of PDB 2qd3 Chain A

Receptor sequence
>2qd3A (length=359) Species: 9606 (Homo sapiens) [Search protein sequence]
RKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKR
RTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFR
YVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVG
RKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHS
LPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQ
TDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVEN
IRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRET
KSFFTSQQL
3D structure
PDB2qd3 A pi-Helix Switch Selective for Porphyrin Deprotonation and Product Release in Human Ferrochelatase.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M76 L92 L98
Catalytic site (residue number reindexed from 1) M12 L28 L34
Enzyme Commision number 4.98.1.1: protoporphyrin 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 FES A C196 S402 C403 C406 C411 C132 S338 C339 C342 C347
Gene Ontology
Molecular Function
GO:0004325 ferrochelatase activity
Biological Process
GO:0006783 heme biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qd3, PDBe:2qd3, PDBj:2qd3
PDBsum2qd3
PubMed17884090
UniProtP22830|HEMH_HUMAN Ferrochelatase, mitochondrial (Gene Name=FECH)

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