Structure of PDB 2ord Chain A Binding Site BS01

Receptor Information
>2ord Chain A (length=393) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KIHHHHHHMYLMNTYSRFPATFVYGKGSWIYDEKGNAYLDFTSGIAVNVL
GHSHPRLVEAIKDQAEKLIHCSNLFWNRPQMELAELLSKNTFGGKVFFAN
TGTEANEAAIKIARKYGKKKSEKKYRILSAHNSFHGRTLGSLTATGQPKY
QKPFEPLVPGFEYFEFNNVEDLRRKMSEDVCAVFLEPIQGESGIVPATKE
FLEEARKLCDEYDALLVFDEVQCGMGRTGKLFAYQKYGVVPDVLTTAKGL
GGGVPIGAVIVNERANVLEPGDHGTTFGGNPLACRAGVTVIKELTKEGFL
EEVEEKGNYLMKKLQEMKEEYDVVADVRGMGLMIGIQFREEVSNREVATK
CFENKLLVVPAGNNTIRFLPPLTVEYGEIDLAVETLKKVLQGI
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 chain2ord Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2ord Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from Thermotoga maritima at 1.40 A resolution
Resolution1.4 Å
Binding residue
(original residue number in PDB)		G94 T95 F126 H127 E178 D211 V213 Q214 K240
Binding residue
(residue number reindexed from 1)		G102 T103 F134 H135 E186 D219 V221 Q222 K248
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F126 E178 D211 Q214 K240 T268 R359
Catalytic site (residue number reindexed from 1) F134 E186 D219 Q222 K248 T276 R367
Enzyme Commision number 2.6.1.11: acetylornithine transaminase.
Gene Ontology
Molecular Function
GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
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
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:2ord, PDBe:2ord, PDBj:2ord
PDBsum2ord
PubMed
UniProtQ9X2A5|ARGD_THEMA Acetylornithine aminotransferase (Gene Name=argD)

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