Structure of PDB 1qnv Chain A Binding Site BS01

Receptor Information

>1qnv Chain A (length=328) Species: 4932 (Saccharomyces cerevisiae)

MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDN
PDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDP
VGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDG
TINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAH
KTFVLSYAAKFSGNLYGPFCYQLPPAGRGLARRALERDMSEGADGIIVKP
STFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAAEKGVVDLKTIAFES
HQGFLRAGARLIITYLAPEFLDWLDEEN

Ligand information

• Ligand ID: PB
• InChI: InChI=1S/Pb/q+2
• InChIKey: RVPVRDXYQKGNMQ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.370: [Pb++]
  : valence
  OpenEye OEToolkits 1.7.2: [Pb+2]
• Formula: Pb
• Name: LEAD (II) ION
• PDB chain: 1qnv Chain A Residue 400

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1qnv MAD Analyses of Yeast 5-Aminolaevulinic Acid Dehydratase. Their Use in Structure Determination and in Defining the Metal Binding Sites
• Resolution: 2.5 Å
• Binding residue (original residue number in PDB): C133 C135 C143 S179
• Binding residue (residue number reindexed from 1): C133 C135 C143 S179
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): K210 K263
• Catalytic site (residue number reindexed from 1): K210 K249
• Enzyme Commision number: 4.2.1.24: porphobilinogen synthase.

Gene Ontology

Molecular Function

• GO:0004655 porphobilinogen synthase activity
• GO:0008270 zinc ion binding
• GO:0016829 lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006782 protoporphyrinogen IX biosynthetic process
• GO:0006783 heme biosynthetic process
• GO:0033014 tetrapyrrole biosynthetic process

Cellular Component

• GO:0005634 nucleus
• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1qnv, PDBe:1qnv, PDBj:1qnv
• PDBsum: 1qnv
• PubMed: 10739915
• UniProt: P05373|HEM2_YEAST Delta-aminolevulinic acid dehydratase (Gene Name=HEM2)