Structure of PDB 2po5 Chain B Binding Site BS01

Receptor Information
>2po5 Chain B (length=359) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKR
LTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFR
YVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVG
RKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSACS
LPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQ
TDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVEN
IRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRET
KSFFTSQQL
Ligand information
Ligand IDFES
InChIInChI=1S/2Fe.2S
InChIKeyNIXDOXVAJZFRNF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04[Fe]1S[Fe]S1
CACTVS 3.341
OpenEye OEToolkits 1.5.0		S1[Fe]S[Fe]1
FormulaFe2 S2
NameFE2/S2 (INORGANIC) CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain2po5 Chain B Residue 999 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2po5 Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis
Resolution2.2 Å
Binding residue
(original residue number in PDB)		C196 R272 S402 C403 C406 C411
Binding residue
(residue number reindexed from 1)		C132 R208 S338 C339 C342 C347
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) M76 L92 L98 R164 Y165 C263 D340 E343 E347
Catalytic site (residue number reindexed from 1) M12 L28 L34 R100 Y101 C199 D276 E279 E283
Enzyme Commision number 4.98.1.1: protoporphyrin ferrochelatase.
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:2po5, PDBe:2po5, PDBj:2po5
PDBsum2po5
PubMed17567154
UniProtP22830|HEMH_HUMAN Ferrochelatase, mitochondrial (Gene Name=FECH)

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