Structure of PDB 4pga Chain A

Receptor sequence
>4pgaA (length=330) Species: 65406 (Pseudomonas sp. 7A) [Search protein sequence]
KLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANV
RGEQVMQIASESITNDDLLKLGKRVAELADSNDVDGIVITHGTDTLEETA
YFLNLVQKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGV
LVTMNDEIQSGRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRH
TVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAKALIHAGTGNG
SVSSRVVPALQQLRKNGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHD
LNPEKARILAMVAMTKTQDSKELQRIFWEY
3D structure
PDB4pga 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.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 SO4 A G19 T20 S67 G99 T100 D101 G12 T13 S60 G92 T93 D94
BS02 NH4 A E68 D101 E61 D94
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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Cellular Component
External links
PDB RCSB:4pga, PDBe:4pga, PDBj:4pga
PDBsum4pga
PubMed9020792
UniProtP10182|ASPQ_PSES7 Glutaminase-asparaginase (Gene Name=ansB)

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