Structure of PDB 4klr Chain A

Receptor sequence
>4klrA (length=359) Species: 9606 (Homo sapiens) [Search protein sequence]
RKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKR
RTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFR
YVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVG
RKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHS
LPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQ
TDESIKGLCERGRKNILLVPIAFTSDHIQTLYELDIEYSQVLAKECGVEN
IRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRET
KSFFTSQQL
3D structure
PDB4klr E343Q variant of human ferrochelatase
ChainA
Resolution2.18 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 Q343 E347
Catalytic site (residue number reindexed from 1) M12 L28 L34 R100 Y101 H199 D276 Q279 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 BCT A M76 L98 Y165 M12 L34 Y101
BS02 HEM A M76 L92 F93 L98 R115 Y123 S197 T198 H263 L265 Y276 F337 I342 M12 L28 F29 L34 R51 Y59 S133 T134 H199 L201 Y212 F273 I278
BS03 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:4klr, PDBe:4klr, PDBj:4klr
PDBsum4klr
PubMed
UniProtP22830|HEMH_HUMAN Ferrochelatase, mitochondrial (Gene Name=FECH)

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