Structure of PDB 2fmn Chain C Binding Site BS01

Receptor Information
>2fmn Chain C (length=271) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRT
HSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGD
LPPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDA
GVNRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFAD
MTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFHFY
TLNRAEMSYAICHTLGVRPGL
Ligand information
Ligand IDFAD
InChIInChI=1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1
InChIKeyVWWQXMAJTJZDQX-UYBVJOGSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P@](O)(=O)O[P@@](O)(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)n5cnc6c(N)ncnc56)c2cc1C
OpenEye OEToolkits 1.5.0Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)n5cnc6c5ncnc6N)O)O)O)O)O
OpenEye OEToolkits 1.5.0Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](CO[P@@](=O)(O)O[P@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)n5cnc6c5ncnc6N)O)O)O)O)O
CACTVS 3.341Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH]([CH](O)[CH]4O)n5cnc6c(N)ncnc56)c2cc1C
ACDLabs 10.04O=C2C3=Nc1cc(c(cc1N(C3=NC(=O)N2)CC(O)C(O)C(O)COP(=O)(O)OP(=O)(O)OCC6OC(n5cnc4c(ncnc45)N)C(O)C6O)C)C
FormulaC27 H33 N9 O15 P2
NameFLAVIN-ADENINE DINUCLEOTIDE
ChEMBLCHEMBL1232653
DrugBankDB03147
ZINCZINC000008215434
PDB chain2fmn Chain C Residue 397 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fmn Structural Perturbations in the Ala -> Val Polymorphism of Methylenetetrahydrofolate Reductase: How Binding of Folates May Protect against Inactivation
Resolution2.05 Å
Binding residue
(original residue number in PDB)		T59 Y60 H88 L117 R118 G119 D120 Y131 A132 A150 Y152 H156 A159 D165 N168 K172 I181 Q183
Binding residue
(residue number reindexed from 1)		T39 Y40 H68 L97 R98 G99 D100 Y106 A107 A125 Y127 H131 A134 D140 N143 K147 I156 Q158
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) S26 E28 D120 F223 H273
Catalytic site (residue number reindexed from 1) S6 E8 D100 F198 H248
Enzyme Commision number 1.5.1.54: methylenetetrahydrofolate reductase (NADH).
Gene Ontology
Molecular Function
GO:0004489 methylenetetrahydrofolate reductase (NAD(P)H) activity
GO:0016491 oxidoreductase activity
GO:0051087 protein-folding chaperone binding
GO:0071949 FAD binding
GO:0106312 methylenetetrahydrofolate reductase (NADH) activity
Biological Process
GO:0006555 methionine metabolic process
GO:0009086 methionine biosynthetic process
GO:0035999 tetrahydrofolate interconversion
Cellular Component
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2fmn, PDBe:2fmn, PDBj:2fmn
PDBsum2fmn
PubMed16605249
UniProtP0AEZ1|METF_ECOLI 5,10-methylenetetrahydrofolate reductase (Gene Name=metF)

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