Structure of PDB 1ylv Chain A

Receptor sequence

>1ylvA (length=341) Species: 4932 (Saccharomyces cerevisiae)

MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDN
PDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDP
VGTAADDPAGPVIQGIKFIREKFPELYIICDVCLCEYTSHGHCGVLYDDG
TINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAH
KTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALE
RDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAA
EKGVVDLKTIAFESHTGFLRAGARLIITYLAPEFLDWLDEE

3D structure

• PDB: 1ylv The Schiff base complex of yeast 5-aminolaevulinic acid dehydratase with laevulinic acid.
• Chain: A
• Resolution: 2.15 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	SHF	A	K210 Y216 F219 K263 Y287 S290	K210 Y216 F219 K263 Y287 S290	PDBbind-CN: -logKd/Ki=2.70,Ki=2.0mM

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:1ylv, PDBe:1ylv, PDBj:1ylv
• PDBsum: 1ylv
• PubMed: 10386874
• UniProt: P05373|HEM2_YEAST Delta-aminolevulinic acid dehydratase (Gene Name=HEM2)