Structure of PDB 1ohl Chain A Binding Site BS01
Receptor Information
>1ohl Chain A (length=340) Species:
4932
(Saccharomyces cerevisiae) [
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MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDN
PDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDP
VGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDG
TINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAH
KTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALE
RDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAA
EKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDE
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1ohl Chain A Residue 400 [
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Receptor-Ligand Complex Structure
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PDB
1ohl
X-Ray Structure of a Putative Reaction Intermediateof 5-Aminolaevulinic Acid Dehydratase
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
C133 C135 C143
Binding residue
(residue number reindexed from 1)
C133 C135 C143
Annotation score
1
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.
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:1ohl
,
PDBe:1ohl
,
PDBj:1ohl
PDBsum
1ohl
PubMed
12777167
UniProt
P05373
|HEM2_YEAST Delta-aminolevulinic acid dehydratase (Gene Name=HEM2)
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