Structure of PDB 1o4s Chain B Binding Site BS01

Receptor Information
>1o4s Chain B (length=384) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KIHHHHHHMVSRRISEIPISKTMELDAKAKALIKKGEDVINLTAGEPDFP
TPEPVVEEAVRFLQKGEVKYTDPRGIYELREGIAKRIGERYKKDISPDQV
VVTNGAKQALFNAFMALLDPGDEVIVFSPVWVSYIPQIILAGGTVNVVET
FMSKNFQPSLEEVEGLLVGKTKAVLINSPNNPTGVVYRREFLEGLVRLAK
KRNFYIISDEVYDSLVYTDEFTSILDVSEGFDRIVYINGFSKSHSMTGWR
VGYLISSEKVATAVSKIQSHTTSCINTVAQYAALKALEVDNSYMVQTFKE
RKNFVVERLKKMGVKFVEPEGAFYLFFKVRGDDVKFCERLLEEKKVALVP
GSAFLKPGFVRLSFATSIERLTEALDRIEDFLNS
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 chain1o4s Chain B Residue 1234 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1o4s Crystal structure of an aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 A resolution
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G97 A98 K99 W123 N173 D201 V203 Y204 S233 K234 R242
Binding residue
(residue number reindexed from 1)		G105 A106 K107 W131 N181 D209 V211 Y212 S241 K242 R250
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W123 D201 V203 K234
Catalytic site (residue number reindexed from 1) W131 D209 V211 K242
Enzyme Commision number 2.6.1.1: aspartate transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
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:1o4s, PDBe:1o4s, PDBj:1o4s
PDBsum1o4s
PubMed15103638
UniProtQ9X0Y2|AAT_THEMA Aspartate aminotransferase (Gene Name=aspC)

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