Structure of PDB 1aw5 Chain A

Receptor sequence
>1aw5A (length=326) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDN
PDDFTEIDSAPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDP
VGTAADDPAGPVIQGIRFIREKFPELYIICDVCLCEYTSHGHCGVLYDDG
TINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAH
KTFVLSYAAKFSGNLYGPACYQLPPAGRGLARRALERDMSEGADGIIVKP
STFYLDIVRDASEICKDLPICAYHVSGEYAMLHAAAEKGVVDLKTIAFES
HQGFLRAGARLIITYLAPEFLDWLDE
3D structure
PDB1aw5 X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K210 K263
Catalytic site (residue number reindexed from 1) K210 K249
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
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1aw5, PDBe:1aw5, PDBj:1aw5
PDBsum1aw5
PubMed9406553
UniProtP05373|HEM2_YEAST Delta-aminolevulinic acid dehydratase (Gene Name=HEM2)

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