Structure of PDB 1szs Chain D

Receptor sequence
>1szsD (length=425) Species: 562 (Escherichia coli) [Search protein sequence]
NSNKELMQRRSQAIPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGQA
VLNTGHLHPKVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDF
AKKTLLVTTGSEAVENAVKIARAATKRSGTIAFSGAYHGRTHYTLALTGK
VNPYSAGMGLMPGHVYRALYPCPLHGISEDDAIASIHRIFKNDAAPEDIA
AIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADEVQSGAGRTGTL
FAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAGN
PIACVAALEVLKVFEQENLLQKANDLGQKLKDGLLAIAEKHPEIGDVRGL
GAMIAIELFEDGDHNKPDAKLTAEIVARARDKGLILLSCGPYYNVLRILV
PLTIEDAQIRQGLEIISQCFDEAKQ
3D structure
PDB1szs Kinetic and Crystallographic Analysis of Active Site Mutants of Escherichia coligamma-Aminobutyrate Aminotransferase.
ChainD
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D G111 S112 Y138 H139 E206 D239 V241 Q242 K268 G110 S111 Y137 H138 E205 D238 V240 Q241 K267
BS02 PMP D G111 S112 Y138 H139 E206 D239 V241 Q242 K268 G110 S111 Y137 H138 E205 D238 V240 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1szs, PDBe:1szs, PDBj:1szs
PDBsum1szs
PubMed15723541
UniProtP22256|GABT_ECOLI 4-aminobutyrate aminotransferase GabT (Gene Name=gabT)

[Back to BioLiP]