Structure of PDB 2qd1 Chain B

Receptor sequence
>2qd1B (length=359) Species: 9606 (Homo sapiens) [Search protein sequence]
RKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKR
RTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFR
YVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVG
RKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHS
LPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQ
TDESIKGLCERGRKNILLVPIAFTSDHIKTLYELDIEYSQVLAKECGVEN
IRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRET
KSFFTSQQL
3D structure
PDB2qd1 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) M76 L92 L98 R164 Y165 H263 D340 K343 E347
Catalytic site (residue number reindexed from 1) M12 L28 L34 R100 Y101 H199 D276 K279 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 C196 R272 S402 C403 C406 C411 C132 R208 S338 C339 C342 C347
BS02 PP9 B M76 L92 L98 M99 R115 I119 Y123 S130 T198 H263 P266 Y276 W310 H341 I342 K343 M12 L28 L34 M35 R51 I55 Y59 S66 T134 H199 P202 Y212 W246 H277 I278 K279
Gene Ontology
Molecular Function
GO:0004325 ferrochelatase activity
Biological Process
GO:0006783 heme biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2qd1, PDBe:2qd1, PDBj:2qd1
PDBsum2qd1
PubMed17884090
UniProtP22830|HEMH_HUMAN Ferrochelatase, mitochondrial (Gene Name=FECH)

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