Structure of PDB 1b4e Chain A

Receptor sequence
>1b4eA (length=323) Species: 562 (Escherichia coli) [Search protein sequence]
TDLSQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEAMP
GVMRIPEKHLAREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVAR
MSRICKQTVPEMIVMSDTCFCEYTSHGHCGVLKEHGVDNDATLENLGKQA
VVAAAAGADFIAPSAAMDGQVQAIRQALDAAGFKDTAIMSYSTKFASSFY
GPFREAAGSALKGDRKSYQMNPMNRREAIRESLLDEAQGADCLMVKPAGA
YLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAIDEEKVVLESLGSI
KRAGADLIFSYFALDLAEKKILR
3D structure
PDB1b4e X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K195 K247
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 E40 H84 E39 H83
BS02 ZN A C120 C122 C130 C119 C121 C129
BS03 SHF A F79 K195 Y201 F204 K247 Y270 V272 S273 Y312 F78 K194 Y200 F203 K246 Y269 V271 S272 Y311 BindingDB: Ki=2.200e+6nM
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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Molecular Function
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Cellular Component
External links
PDB RCSB:1b4e, PDBe:1b4e, PDBj:1b4e
PDBsum1b4e
PubMed10194344
UniProtP0ACB2|HEM2_ECOLI Delta-aminolevulinic acid dehydratase (Gene Name=hemB)

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