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Structure of PDB 5lnw Chain D Binding Site BS02

Receptor Information
>5lnw Chain D (length=262) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQ
GGVARMSDPQMIKEIKQAVTIPVMAKARIGHFVEAQILEAIGIDYIDESE
VLTLADEDHHINKHNFRIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTG
NIIEAVRHVRSVNGDIRVLRNMDDDEVFTFAKKLAAPYDLVMQTKQLGRL
PVVQFAAGGVATPADAALMMQLGCDGVFVGSGIFPARRARAIVQAVTHYS
DPEMLVEVSCGL
Ligand information
Ligand IDRP5
InChIInChI=1S/C5H11O8P/c6-3-2(1-12-14(9,10)11)13-5(8)4(3)7/h2-8H,1H2,(H2,9,10,11)/t2-,3-,4-,5-/m1/s1
InChIKeyKTVPXOYAKDPRHY-TXICZTDVSA-N
SMILES
SoftwareSMILES
CACTVS 3.370O[CH]1O[CH](CO[P](O)(O)=O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.0C([C@@H]1[C@H]([C@H]([C@@H](O1)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.7.0C(C1C(C(C(O1)O)O)O)OP(=O)(O)O
CACTVS 3.370O[C@@H]1O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]1O
ACDLabs 12.01O=P(O)(O)OCC1OC(O)C(O)C1O
FormulaC5 H11 O8 P
Name5-O-phosphono-beta-D-ribofuranose;
[(2R,3S,4S,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN PHOSPHATE;
5-O-phosphono-beta-D-ribose;
5-O-phosphono-D-ribose;
5-O-phosphono-ribose
ChEMBLCHEMBL1235722
DrugBankDB04352
ZINCZINC000004228241
PDB chain5lnw Chain D Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5lnw Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis.
Resolution1.9 Å
Binding residue
(original residue number in PDB)
H132 R154 R155
Binding residue
(residue number reindexed from 1)
H110 R132 R133
Annotation score1
Enzymatic activity
Enzyme Commision number 4.3.3.6: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing).
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0036381 pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
GO:0042803 protein homodimerization activity
GO:0046982 protein heterodimerization activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006979 response to oxidative stress
GO:0006982 response to lipid hydroperoxide
GO:0009651 response to salt stress
GO:0010224 response to UV-B
GO:0010335 response to non-ionic osmotic stress
GO:0015994 chlorophyll metabolic process
GO:0042538 hyperosmotic salinity response
GO:0042819 vitamin B6 biosynthetic process
GO:0042823 pyridoxal phosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0012505 endomembrane system

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5lnw, PDBe:5lnw, PDBj:5lnw
PDBsum5lnw
PubMed28092359
UniProtQ8L940|PDX13_ARATH Pyridoxal 5'-phosphate synthase subunit PDX1.3 (Gene Name=PDX13)

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