Structure of PDB 1gjp Chain A

Receptor sequence

>1gjpA (length=340) Species: 4932 (Saccharomyces cerevisiae)

MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDN
PDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDP
VGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDG
TINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAH
KTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALE
RDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAA
EKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDE

3D structure

• PDB: 1gjp The X-Ray Structure of Yeast 5-Aminolaevulinic Acid Dehydratase Complexed with Two Diacid Inhibitors
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

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

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	4OX	A	S179 Y207 K210 F219 K263 Y287 S290 Y329	S179 Y207 K210 F219 K263 Y287 S290 Y329
BS02	ZN	A	C133 C135 C143	C133 C135 C143

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:1gjp, PDBe:1gjp, PDBj:1gjp
• PDBsum: 1gjp
• PubMed: 11513881
• UniProt: P05373|HEM2_YEAST Delta-aminolevulinic acid dehydratase (Gene Name=HEM2)