Structure of PDB 5bj3 Chain B Binding Site BS01

Receptor Information
>5bj3 Chain B (length=363) Species: 271 (Thermus aquaticus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRGLSRRVQAMKPLVALTAGEPDFDTPEHVKEAARRALAQGKTKYAPPAG
IPELREALAEKFRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVI
VLSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRAITPRTKALV
VNSPNNPTGAVYPKEVLEALARLAVEHDFYLVSDEIYEHLLYEGEHFSPG
RVAPEHTLTVNGAAKAFAMTGWRIGYACGPKEVIKAMASVSRQSTTSPDT
IAQWATLEALTNQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSG
AFYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHVRLSYATSEE
NLRKALERFARVL
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 chain5bj3 Chain B Residue 413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5bj3 Substrate recognition mechanism of thermophilic dual-substrate enzyme
Resolution2.2 Å
Binding residue
(original residue number in PDB)		G99 G100 S101 W125 N175 D203 I205 Y206 A233 K234 R242
Binding residue
(residue number reindexed from 1)		G80 G81 S82 W106 N156 D184 I186 Y187 A214 K215 R223
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W125 D203 I205 K234
Catalytic site (residue number reindexed from 1) W106 D184 I186 K215
Enzyme Commision number 2.6.1.1: aspartate transaminase.
2.6.1.78: aspartate--prephenate aminotransferase.
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
GO:0033853 aspartate-prephenate aminotransferase activity
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:5bj3, PDBe:5bj3, PDBj:5bj3
PDBsum5bj3
PubMed11432784
UniProtQ56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)

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