Structure of PDB 1ohl Chain A

Receptor sequence

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

MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDN
PDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDP
VGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDG
TINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAH
KTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALE
RDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAA
EKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDE

3D structure

• PDB: 1ohl X-Ray Structure of a Putative Reaction Intermediateof 5-Aminolaevulinic Acid Dehydratase
• Chain: A
• Resolution: 1.6 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	ZN	A	C133 C135 C143	C133 C135 C143
BS02	PBG	A	C135 S179 K210 F219 R220 K263 Y287 V289 S290 Y329	C135 S179 K210 F219 R220 K263 Y287 V289 S290 Y329

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:1ohl, PDBe:1ohl, PDBj:1ohl
• PDBsum: 1ohl
• PubMed: 12777167
• UniProt: P05373|HEM2_YEAST Delta-aminolevulinic acid dehydratase (Gene Name=HEM2)