Structure of PDB 4pga Chain A Binding Site BS02
Receptor Information
>4pga Chain A (length=330) Species:
65406
(Pseudomonas sp. 7A) [
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KLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANV
RGEQVMQIASESITNDDLLKLGKRVAELADSNDVDGIVITHGTDTLEETA
YFLNLVQKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGV
LVTMNDEIQSGRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRH
TVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAKALIHAGTGNG
SVSSRVVPALQQLRKNGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHD
LNPEKARILAMVAMTKTQDSKELQRIFWEY
Ligand information
Ligand ID
NH4
InChI
InChI=1S/H3N/h1H3/p+1
InChIKey
QGZKDVFQNNGYKY-UHFFFAOYSA-O
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[NH4+]
Formula
H4 N
Name
AMMONIUM ION
ChEMBL
DrugBank
ZINC
PDB chain
4pga Chain A Residue 339 [
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Receptor-Ligand Complex Structure
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PDB
4pga
Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7 A resolution.
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
E68 D101
Binding residue
(residue number reindexed from 1)
E61 D94
Annotation score
5
Enzymatic activity
Catalytic site (original residue number in PDB)
T20 Y34 T100 D101 K173 E294
Catalytic site (residue number reindexed from 1)
T13 Y27 T93 D94 K166 E287
Enzyme Commision number
3.5.1.38
: glutamin-(asparagin-)ase.
Gene Ontology
Molecular Function
GO:0004067
asparaginase activity
GO:0004359
glutaminase activity
GO:0016787
hydrolase activity
GO:0050417
glutamin-(asparagin-)ase activity
Biological Process
GO:0006520
amino acid metabolic process
GO:0006528
asparagine metabolic process
Cellular Component
GO:0042597
periplasmic space
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:4pga
,
PDBe:4pga
,
PDBj:4pga
PDBsum
4pga
PubMed
9020792
UniProt
P10182
|ASPQ_PSES7 Glutaminase-asparaginase (Gene Name=ansB)
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