Structure of PDB 1i8j Chain A

Receptor sequence
>1i8jA (length=323) Species: 562 (Escherichia coli) [Search protein sequence]
TDLIQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEAMP
GVMRIPEKHLAREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVAR
MSRICKQTVPEMIVMSDTCFCEYTSHGHCGVLCEHGVDNDATLENLGKQA
VVAAAAGADFIAPSAAMDGQVQAIRQALDAAGFKDTAIMSYSTKFASSFY
GPFREAAGSALKGDRKSYQMNPMNRREAIRESLLDEAQGADCLMVKPAGA
YLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAIDEEKVVLESLGSI
KRAGADLIFSYFALDLAEKKILR
3D structure
PDB1i8j Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 DSB A K194 Y200 F203 R204 R215 Q219 K246 Y269 V271 S272 Y311 K194 Y200 F203 R204 R215 Q219 K246 Y269 V271 S272 Y311 PDBbind-CN: -logKd/Ki=4.41,IC50=39uM
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

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Cellular Component
External links
PDB RCSB:1i8j, PDBe:1i8j, PDBj:1i8j
PDBsum1i8j
PubMed11444968
UniProtP0ACB2|HEM2_ECOLI Delta-aminolevulinic acid dehydratase (Gene Name=hemB)

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