Structure of PDB 2qd2 Chain A Binding Site BS01

Receptor Information

>2qd2 Chain A (length=359) Species: 9606 (Homo sapiens)

RKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPAIAKR
RTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFR
YVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVG
RKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHS
LPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQ
TDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVEN
IRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRET
KSFFTSQQL

Ligand information

• Ligand ID: BCT
• InChI: InChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-1
• InChIKey: BVKZGUZCCUSVTD-UHFFFAOYSA-M
• SMILES:
  OpenEye OEToolkits 1.5.0: C(=O)(O)[O-]
  CACTVS 3.341: OC([O-])=O
  ACDLabs 10.04: [O-]C(=O)O
• Formula: C H O3
• Name: BICARBONATE ION
• PDB chain: 2qd2 Chain A Residue 1

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2qd2 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): L98 Y165
• Binding residue (residue number reindexed from 1): L34 Y101
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): M76 L92 L98 R164 Y165 H263 D340 E343 E347
• 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.

Gene Ontology

Molecular Function

• GO:0004325 ferrochelatase activity

Biological Process

• GO:0006783 heme biosynthetic process

External links

• PDB: RCSB:2qd2, PDBe:2qd2, PDBj:2qd2
• PDBsum: 2qd2
• PubMed: 17884090
• UniProt: P22830|HEMH_HUMAN Ferrochelatase, mitochondrial (Gene Name=FECH)