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BioLiP

Structure of PDB 1tdj Chain A Binding Site BS01

Receptor Information
>1tdj Chain A (length=494) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKRED
RQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVK
ALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWV
PPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGGLAAGVAVLIKQLM
PQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRL
CQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHN
IRGERLAHILSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKGSFLK
FCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQMLNDGGY
SVVDLSDDEMAKLHVRYMVGGRPSHPLQERLYSFEFPESPGALLRFLNTL
GTYWNISLFHYRSHGTDYGRVLAAFEYDCHDETNNPAFRFFLAG
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 chain1tdj Chain A Residue 962 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1tdj Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		F61 K62 N89 G188 G189 G190 G191 G241 E286 S315 G316
Binding residue
(residue number reindexed from 1)		F57 K58 N85 G184 G185 G186 G187 G237 E282 S311 G312
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K62 A87 E213 S217 C219 G241 L314 S315
Catalytic site (residue number reindexed from 1) K58 A83 E209 S213 C215 G237 L310 S311
Enzyme Commision number 4.3.1.19: threonine ammonia-lyase.
Gene Ontology
Molecular Function
GO:0003941 L-serine ammonia-lyase activity
GO:0004794 threonine deaminase activity
GO:0016597 amino acid binding
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006565 L-serine catabolic process
GO:0006566 threonine metabolic process
GO:0006567 threonine catabolic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009097 isoleucine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1tdj, PDBe:1tdj, PDBj:1tdj
PDBsum1tdj
PubMed9562556
UniProtP04968|ILVA_ECOLI L-threonine dehydratase biosynthetic IlvA (Gene Name=ilvA)

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