Structure of PDB 1l6y Chain A

Receptor sequence

>1l6yA (length=323) Species: 562 (Escherichia coli)

TDLIQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEAMP
GVMRIPEKHLAREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVAR
MSRICKQTVPEMIVMSDTCFCEYTSHGHCGVLCEHGVDNDATLENLGKQA
VVAAAAGADFIAPSAAMDGQVQAIRQALDAAGFKDTAIMSYSTKFASSFY
GPFREAAGSALKGDRKSYQMNPMNRREAIRESLLDEAQGADCLMVKPAGA
YLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAIDEEKVVLESLGSI
KRAGADLIFSYFALDLAEKKILR

3D structure

• PDB: 1l6y Species-Specific Inhibition of Porphobilinogen Synthase by 4-Oxosebacic Acid
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K194 K246
• Catalytic site (residue number reindexed from 1): K194 K246
• 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	C119 C121 C129	C119 C121 C129
BS02	4OX	A	K194 Y200 F203 R204 R215 Q219 K246 V271 S272 Y311	K194 Y200 F203 R204 R215 Q219 K246 V271 S272 Y311	PDBbind-CN: -logKd/Ki=3.66,IC50=0.22mM

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• 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:0005829 cytosol

External links

• PDB: RCSB:1l6y, PDBe:1l6y, PDBj:1l6y
• PDBsum: 1l6y
• PubMed: 11909869
• UniProt: P0ACB2|HEM2_ECOLI Delta-aminolevulinic acid dehydratase (Gene Name=hemB)