Structure of PDB 4atq Chain D

Receptor sequence
>4atqD (length=441) Species: 290340 (Paenarthrobacter aurescens TC1) [Search protein sequence]
SYRIEQKRNINGAFPGPKSQALAERRSAVVAAGVASGVPVYVEDADGGII
RDVDGNSFIDLGSGIAVTSVGASDPAVVAAVQEAAAHFTHTCFMVTPYEG
YVAVTEQLNRLTPGDHAKRTVLFNSGAEAVENAVKVARLATGRDAVVAFD
HAYHGRTNLTMALTAKAMPYKTNFGPFAPEVYRMPMSYPFREENPEITGA
EAAKRAITMIEKQIGGDQVAAIIIEPIQGEGGFIVPAEGFLPALSEWAKE
KGIVFIADEVQSGFCRTGEWFAVDHEGVVPDIITMAKGIAGGLPLSAITG
RADLLDAVHPGGLGGTYGGNPVACAAALAAIDTMEQHDLNGRARHIEELA
LGKLRELAAESVVGDIRGRGAMLAIELVQPGSKEPNAELTKAVAAACLKE
GVIILTCGTYGNVIRLLPPLVISDELLIDGLEVLAAAIKAH
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.
ChainD
Resolution2.75 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) V42 Y161 E233 D266 Q269 K295 T324 R429
Catalytic site (residue number reindexed from 1) V34 Y153 E225 D258 Q261 K287 T316 R415
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 D S133 G134 A135 Y161 H162 E233 D266 V268 S125 G126 A127 Y153 H154 E225 D258 V260
BS02 ABU D Y161 R164 E238 K295 Y153 R156 E230 K287
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

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

[Back to BioLiP]