Structure of PDB 2qd3 Chain A Binding Site BS01

Receptor Information

>2qd3 Chain A (length=359) Species: 9606 (Homo sapiens)

RKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKR
RTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFR
YVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVG
RKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHS
LPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQ
TDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVEN
IRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRET
KSFFTSQQL

Ligand information

• Ligand ID: FES
• InChI: InChI=1S/2Fe.2S
• InChIKey: NIXDOXVAJZFRNF-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04: [Fe]1S[Fe]S1
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: S1[Fe]S[Fe]1
• Formula: Fe2 S2
• Name: FE2/S2 (INORGANIC) CLUSTER
• PDB chain: 2qd3 Chain A Residue 601

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2qd3 A pi-Helix Switch Selective for Porphyrin Deprotonation and Product Release in Human Ferrochelatase.
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): C196 S402 C403 C406 C411
• Binding residue (residue number reindexed from 1): C132 S338 C339 C342 C347
• Annotation score: 1

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.

Gene Ontology

Molecular Function

• GO:0004325 ferrochelatase activity

Biological Process

• GO:0006783 heme biosynthetic process

External links

• PDB: RCSB:2qd3, PDBe:2qd3, PDBj:2qd3
• PDBsum: 2qd3
• PubMed: 17884090
• UniProt: P22830|HEMH_HUMAN Ferrochelatase, mitochondrial (Gene Name=FECH)