Structure of PDB 1vef Chain B

Receptor sequence
>1vefB (length=387) Species: 274 (Thermus thermophilus) [Search protein sequence]
WRALLEAEKTLDSGVYNKHDLLIVRGQGARVWDAEGNEYIDCVGGYGVAN
LGHGNPEVVEAVKRQAETLMAMPQTLPTPMRGEFYRTLTAILPPELNRVF
PVNSGTEANEAALKFARAHTGRKKFVAAMRGFSGRTMGSLSVTWEPKYRE
PFLPLVEPVEFIPYNDVEALKRAVDEETAAVILEPVQGEGGVRPATPEFL
RAAREITQEKGALLILDEIQTGMGRTGKRFAFEHFGIVPDILTLAKALGG
GVPLGVAVMREEVARSMPKGGHGTTFGGNPLAMAAGVAAIRYLERTRLWE
RAAELGPWFMEKLRAIPSPKIREVRGMGLMVGLELKEKAAPYIARLEKEH
RVLALQAGPTVIRFLPPLVIEKEDLERVVEAVRAVLA
3D structure
PDB1vef Three-Dimensional Strutcure of Acetylornithine aminotransferase from Thermus thermophilus HB8
ChainB
Resolution1.35 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) S1021 F1140 E1192 D1225 Q1228 K1254 T1283 R1371
Catalytic site (residue number reindexed from 1) S13 F132 E184 D217 Q220 K246 T275 R363
Enzyme Commision number 2.6.1.118: [amino group carrier protein]-gamma-(L-lysyl)-L-glutamate aminotransferase.
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 B G1113 T1114 F1140 S1141 E1192 D1225 I1227 K1254 G105 T106 F132 S133 E184 D217 I219 K246
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0006525 arginine metabolic process
GO:0006526 L-arginine biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0019878 lysine biosynthetic process via aminoadipic acid
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1vef, PDBe:1vef, PDBj:1vef
PDBsum1vef
PubMed
UniProtQ5SHH5|LYSJ_THET8 [LysW]-aminoadipate semialdehyde transaminase (Gene Name=lysJ)

[Back to BioLiP]