Structure of PDB 1szu Chain B

Receptor sequence
>1szuB (length=425) Species: 562 (Escherichia coli) [Search protein sequence]
NSNKELMQRRSQAIPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIA
VLNTGHLHPKVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDF
AKKTLLVTTGSEAVENAVKIARAATKRSGTIAFSGAYHGRTHYTLALTGK
VNPYSAGMGLMPGHVYRALYPCPLHGISEDDAIASIHRIFKNDAAPEDIA
AIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADEAQSGAGRTGTL
FAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAGN
PIACVAALEVLKVFEQENLLQKANDLGQKLKDGLLAIAEKHPEIGDVRGL
GAMIAIELFEDGDHNKPDAKLTAEIVARARDKGLILLSCGPYYNVLRILV
PLTIEDAQIRQGLEIISQCFDEAKQ
3D structure
PDB1szu Kinetic and Crystallographic Analysis of Active Site Mutants of Escherichia coligamma-Aminobutyrate Aminotransferase.
ChainB
Resolution2.52 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V19 Y138 E206 D239 Q242 K268 T297 R398
Catalytic site (residue number reindexed from 1) V18 Y137 E205 D238 Q241 K267 T296 R397
Enzyme Commision number 2.6.1.19: 4-aminobutyrate--2-oxoglutarate transaminase.
2.6.1.48: 5-aminovalerate transaminase.
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 PLP B T110 G111 S112 Y138 H139 E206 D239 A241 Q242 K268 T109 G110 S111 Y137 H138 E205 D238 A240 Q241 K267
BS02 PMP B G111 S112 Y138 H139 E206 D239 A241 Q242 K268 G110 S111 Y137 H138 E205 D238 A240 Q241 K267
Gene Ontology
Molecular Function
GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0034386 4-aminobutyrate:2-oxoglutarate transaminase activity
GO:0042803 protein homodimerization activity
GO:0047589 5-aminovalerate transaminase activity
Biological Process
GO:0009448 gamma-aminobutyric acid metabolic process
GO:0009450 gamma-aminobutyric acid catabolic process
GO:0042450 arginine biosynthetic process via ornithine
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:1szu, PDBe:1szu, PDBj:1szu
PDBsum1szu
PubMed15723541
UniProtP22256|GABT_ECOLI 4-aminobutyrate aminotransferase GabT (Gene Name=gabT)

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