Structure of PDB 3ia4 Chain C Binding Site BS01

Receptor Information
>3ia4 Chain C (length=160) Species: 111291 (Moritella profunda) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIVSMIAALANNRVIGLDNKMPWHLPAELQLFKRATLGKPIVMGRNTFES
IGRPLPGRLNIVLSRQDYQPEGVTVVATLEDAVVAAGDVEELMIIGGATI
YNQCLAAADRLYLTHIELTTEGDTWFPDYEQYNWQEIEHESYAADDKNPH
NYRFSLLERV
Ligand information
Ligand IDNDP
InChIInChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyACFIXJIJDZMPPO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
FormulaC21 H30 N7 O17 P3
NameNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
ChEMBLCHEMBL407009
DrugBankDB02338
ZINCZINC000008215411
PDB chain3ia4 Chain C Residue 163 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3ia4 Are the Catalytic Properties of Enzymes from Piezophilic Organisms Pressure Adapted?
Resolution1.7 Å
Binding residue
(original residue number in PDB)		A7 A8 I15 N19 K20 M21 G44 R45 N46 T47 L63 S64 R65 A78 I96 G98 A99 T100 I101 Q104 T125
Binding residue
(residue number reindexed from 1)		A7 A8 I15 N19 K20 M21 G44 R45 N46 T47 L63 S64 R65 A77 I95 G97 A98 T99 I100 Q103 T124
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) I6 M21 W23 E28 L29 F32 L55 L93 T115
Catalytic site (residue number reindexed from 1) I6 M21 W23 E28 L29 F32 L55 L92 T114
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ia4, PDBe:3ia4, PDBj:3ia4
PDBsum3ia4
PubMed19681091
UniProtQ70YQ6

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