Structure of PDB 2qd3 Chain B

Receptor sequence
>2qd3B (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.
ChainB
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) M576 L592 L598 R664 Y665 H763 D840 E843 E847
Catalytic site (residue number reindexed from 1) M12 L28 L34 R100 Y101 H199 D276 E279 E283
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 B C696 R772 S902 C903 C906 C911 C132 R208 S338 C339 C342 C347
BS02 HEM B F588 R615 I619 Y623 S697 T698 H763 P766 I842 E843 F24 R51 I55 Y59 S133 T134 H199 P202 I278 E279
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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