Structure of PDB 1b5t Chain A Binding Site BS01
Receptor Information
>1b5t Chain A (length=275) Species:
562
(Escherichia coli) [
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GQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRT
HSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGD
LPPGSGKPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLK
RKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQA
KKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVK
DFHFYTLNRAEMSYAICHTLGVRPA
Ligand information
Ligand ID
FAD
InChI
InChI=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
InChIKey
VWWQXMAJTJZDQX-UYBVJOGSSA-N
SMILES
Software
SMILES
CACTVS 3.341
Cc1cc2N=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 1.5.0
Cc1cc2c(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 1.5.0
Cc1cc2c(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 3.341
Cc1cc2N=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 10.04
O=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
Formula
C27 H33 N9 O15 P2
Name
FLAVIN-ADENINE DINUCLEOTIDE
ChEMBL
CHEMBL1232653
DrugBank
DB03147
ZINC
ZINC000008215434
PDB chain
1b5t Chain A Residue 395 [
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Receptor-Ligand Complex Structure
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PDB
1b5t
The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
Y60 H88 L117 R118 G119 D120 Y131 A132 A150 Y152 H156 E158 A159 D165 N168 R171 K172
Binding residue
(residue number reindexed from 1)
Y40 H68 L97 R98 G99 D100 Y111 A112 A130 Y132 H136 E138 A139 D145 N148 R151 K152
Annotation score
2
Enzymatic activity
Catalytic site (original residue number in PDB)
S26 E28 D120 F223 H273
Catalytic site (residue number reindexed from 1)
S6 E8 D100 F203 H253
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:1b5t
,
PDBe:1b5t
,
PDBj:1b5t
PDBsum
1b5t
PubMed
10201405
UniProt
P0AEZ1
|METF_ECOLI 5,10-methylenetetrahydrofolate reductase (Gene Name=metF)
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