Structure of PDB 6j2v Chain B

Receptor sequence
>6j2vB (length=440) Species: 196627 (Corynebacterium glutamicum ATCC 13032) [Search protein sequence]
LSYRIPQSRTVAEQVPGPKSKALDERRQAAVARALAPGLPGYVVDADGGI
LADADGNRFIDLASGIAVTTVGGSNAAVAKAVGAAAARFTHTCFMVSPYE
TYVAMAERLNALTPGDHDKKSALFNSGAEAVENAVKVARAYTGKGAVVVF
DNAYHGRTNLTMAMTAKNRPYKSGFGPLAADVYRAPMSYPLRDGLSGPEA
AERAISVIESQVGAENLACVVIEPIQGEGGFIVPAPGFLAAISTWCREND
VVFIADEIQSGFLRTGDWFASDAEGVIPDVITTAKGIAGGMPLSAVTGRA
EIMDAPGPGALGGTYGGNPVACAAALAAIEVMEQADLKTRAQEIETIIRD
EFAQLSAFPEVAEIRGRGAMMAIELIDATGRPNAALTAAVAARAKAEGVL
LLTCGTDGNVIRLLPPLVIAEDTLRDGLQVLVAALERETA
3D structure
PDB6j2v Crystal structure of gamma-aminobutyrate aminotransferase in complex with a PLP-GABA adduct from Corynebacterium glutamicum.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L38 Y157 D259 K288
Catalytic site (residue number reindexed from 1) L35 Y154 D256 K285
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 PLZ B M98 G316 T317 M95 G313 T314
BS02 PLZ B G130 A131 Y157 H158 R160 E226 D259 I261 K288 G127 A128 Y154 H155 R157 E223 D256 I258 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:6j2v, PDBe:6j2v, PDBj:6j2v
PDBsum6j2v
PubMed31072617
UniProtQ8NT35

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