Structure of PDB 4atq Chain E

Receptor sequence
>4atqE (length=442) Species: 290340 (Paenarthrobacter aurescens TC1) [Search protein sequence]
ELSYRIEQKRNINGAFPGPKSQALAERRSAVVAAGVASGVPVYVEDADGG
IIRDVDGNSFIDLGSGIAVTSVGASDPAVVAAVQEAAAHFTHTCFMVTPY
EGYVAVTEQLNRLTPGDHAKRTVLFNSGAEAVENAVKVARLATGRDAVVA
FDHAYHGRTNLTMALTAKAMPYKTNFGPFAPEVYRMPMSYPFREENPEIT
GAEAAKRAITMIEKQIGGDQVAAIIIEPIQGEGGFIVPAEGFLPALSEWA
KEKGIVFIADEVQSGFCRTGEWFAVDHEGVVPDIITMAKGIAGGLPLSAI
TGRADLLDAVHPGGLGGTYGGNPVACAAALAAIDTMEQHDLNGRARHIEE
LALGKLRELAASVVGDIRGRGAMLAIELVQPGSKEPNAELTKAVAAACLK
EGVIILTCGTYGNVIRLLPPLVISDELLIDGLEVLAAAIKAH
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.
ChainE
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) V36 Y155 E227 D260 Q263 K289 T318 R416
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 E G134 A135 Y161 H162 E233 D266 V268 Q269 G128 A129 Y155 H156 E227 D260 V262 Q263
BS02 ABU E Y161 R164 E238 K295 Y155 R158 E232 K289
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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