Structure of PDB 1w5o Chain A Binding Site BS01
Receptor Information
>1w5o Chain A (length=329) Species:
208964
(Pseudomonas aeruginosa PAO1) [
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NRAYPYTRLRRNRRDDFSRRLVRENVLTVDDLILPVFVLDGVNQRESIPS
MPGVERLSIDQLLIEAEEWVALGIPALALFPVTPVEKKSLDAAEAYNPEG
IAQRATRALRERFPELGIITDVCLCPFTTHGQCGILDDDGYVLNDVSIDV
LVRQALSHAEAGAQVVAPSDMMDGRIGAIREALESAGHTNVRVMAYSAKY
ASAYYGPFRDAVGSASNLGKGNKATYQMDPANSDEALHEVAADLAEGADM
VMVKPGMPYLDIVRRVKDEFRAPTFVYQVSGEYAMHMGAIQNGWLAESVI
LESLTAFKRAGADGILTYFAKQAAEQLRR
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
1w5o Chain A Residue 1339 [
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Receptor-Ligand Complex Structure
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PDB
1w5o
Tracking the Evolution of Porphobilinogen Synthase Metal Dependence in Vitro
Resolution
1.85 Å
Binding residue
(original residue number in PDB)
C129 C131 C139
Binding residue
(residue number reindexed from 1)
C123 C125 C133
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
K205 K260
Catalytic site (residue number reindexed from 1)
K199 K254
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:0006779
porphyrin-containing compound biosynthetic 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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Biological Process
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Cellular Component
External links
PDB
RCSB:1w5o
,
PDBe:1w5o
,
PDBj:1w5o
PDBsum
1w5o
PubMed
15644204
UniProt
Q59643
|HEM2_PSEAE Delta-aminolevulinic acid dehydratase (Gene Name=hemB)
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