Structure of PDB 4h98 Chain B Binding Site BS01

Receptor Information
>4h98 Chain B (length=224) Species: 284593 (Nakaseomyces glabratus CBS 138) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VPVVGIVAALLPEMGIGFQGNLPWRLAKEMKYFREVTTLTNDNSKQNVVI
MGRKTWESIPQKFRPLPKRINVVVSRSFDGELRKVEDGIYHSNSLRNCLT
ALQSSLANENKIERIYIIGGGEIYRQSMDLADHWLITKIMPLPETTIPQM
DTFLQKQELEQRFYDNSDKLVDFLPSSIQLEGRLTSQEWNGELVKGLPVQ
EKGYQFYFTLYTKKLEHHHHHHHH
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 chain4h98 Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4h98 Structural analysis of the active sites of dihydrofolate reductase from two species of Candida uncovers ligand-induced conformational changes shared among species.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		V10 A11 I19 G23 N24 L25 G55 R56 K57 T58 V77 S78 R79 N96 I121 G123 G124 E125 I126 Q129
Binding residue
(residue number reindexed from 1)		V7 A8 I16 G20 N21 L22 G52 R53 K54 T55 V74 S75 R76 N93 I118 G120 G121 E122 I123 Q126
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) L25 W27 E32 M33 F36 L69 I118 T140
Catalytic site (residue number reindexed from 1) L22 W24 E29 M30 F33 L66 I115 T137
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:0005575 cellular_component
GO:0005739 mitochondrion

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4h98, PDBe:4h98, PDBj:4h98
PDBsum4h98
PubMed23375226
UniProtQ6FPH0

[Back to BioLiP]