Structure of PDB 4atq Chain L

Receptor sequence
>4atqL (length=436) Species: 290340 (Paenarthrobacter aurescens TC1) [Search protein sequence]
RIEQKRNINGAFPGPKSQALAERRSAVVAAGVASGVPVYVEDADGGIIRD
VDGNSFIDLGSGIAVTSVGASDPAVVAAVQEAAAHFTHTCFMVTPYEGYV
AVTEQLNRLTPGDHAKRTVLFNSGAEAVENAVKVARLATGRDAVVAFDHA
YHGRTNLTMALTAKAMPYKTNFGPFAPEVYRMPMSYPFREENPEITGAEA
AKRAITMIEKQIGGDQVAAIIIEPIQGEGGFIVPAEGFLPALSEWAKEKG
IVFIADEVQSGFCRTGEWFAVDHEGVVPDIITMAKGIAGGLPLSAITGRA
DLLDAVHPGGLGGTYGGNPVACAAALAAIDTMEQHDLNGRARHIEELALG
KLRELSVVGDIRGRGAMLAIELVQPGSKEPNAELTKAVAAACLKEGVIIL
TCGTYGNVIRLLPPLVISDELLIDGLEVLAAAIKAH
3D structure
PDB4atq Structures of a Gamma-Aminobutyrate (Gaba) Transaminase from the S-Triazine-Degrading Organism Arthrobacter Aurescens Tc1 in Complex with Plp and with its External Aldimine Plp- Gaba Adduct.
ChainL
Resolution2.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V42 Y161 E233 D266 Q269 K295 T324 R429
Catalytic site (residue number reindexed from 1) V32 Y151 E223 D256 Q259 K285 T314 R410
Enzyme Commision number 2.6.1.19: 4-aminobutyrate--2-oxoglutarate 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 L S133 G134 A135 Y161 H162 E233 D266 S123 G124 A125 Y151 H152 E223 D256
BS02 ABU L Y161 R164 E238 K295 Y151 R154 E228 K285
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0034386 4-aminobutyrate:2-oxoglutarate transaminase activity
GO:0042802 identical protein binding
Biological Process
GO:0009448 gamma-aminobutyric acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4atq, PDBe:4atq, PDBj:4atq
PDBsum4atq
PubMed23027742
UniProtA1R958

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