Structure of PDB 1vef Chain B Binding Site BS01

Receptor Information
>1vef Chain B (length=387) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
WRALLEAEKTLDSGVYNKHDLLIVRGQGARVWDAEGNEYIDCVGGYGVAN
LGHGNPEVVEAVKRQAETLMAMPQTLPTPMRGEFYRTLTAILPPELNRVF
PVNSGTEANEAALKFARAHTGRKKFVAAMRGFSGRTMGSLSVTWEPKYRE
PFLPLVEPVEFIPYNDVEALKRAVDEETAAVILEPVQGEGGVRPATPEFL
RAAREITQEKGALLILDEIQTGMGRTGKRFAFEHFGIVPDILTLAKALGG
GVPLGVAVMREEVARSMPKGGHGTTFGGNPLAMAAGVAAIRYLERTRLWE
RAAELGPWFMEKLRAIPSPKIREVRGMGLMVGLELKEKAAPYIARLEKEH
RVLALQAGPTVIRFLPPLVIEKEDLERVVEAVRAVLA
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain1vef Chain B Residue 1513 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1vef Three-Dimensional Strutcure of Acetylornithine aminotransferase from Thermus thermophilus HB8
Resolution1.35 Å
Binding residue
(original residue number in PDB)		G1113 T1114 F1140 S1141 E1192 D1225 I1227 K1254
Binding residue
(residue number reindexed from 1)		G105 T106 F132 S133 E184 D217 I219 K246
Annotation score1
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.
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

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

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