Structure of PDB 4l65 Chain A Binding Site BS02

Receptor Information
>4l65 Chain A (length=750) Species: 237561 (Candida albicans SC5314) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVQSSVLGFPRIGGQRELKKITEAYWSGKATVEELLAKGKELREHNWKLQ
QKAGVDIIPSNDFSYYDQVLDLSLLFNAIPERYTKFDLAPIDVLFAMGRG
LQVTALEMVKWFDSNYHYVRPTFSHSTEFKLNTAAGIKPVDEFNEAKALG
VQTRPVILGPVSYLYLGKADKDSLDLEPISLLPKILPVYKELLQKLKEAG
AEQVQIDEPVLVLDLPEAVQSKFKEAYDALVGADVPELILTTYFGDVRPN
LKAIENLPVAGFHFDFVRVPEQLDEVASILKDGQTLSAGVVDGRNIWKTD
FAKASAVVQKAIEKVGKDKVVVATSSSLLHTPVDLESETKLDAVIKDWFS
FATQKLDEVVVIAKNVSGEDVSKQLEANAASIKARSESSITNDPKVQERL
TTINEALATRKAAFPERLTEQKAKYNLPLFPTTTIGSFPQTKDIRINRNK
FAKGQITAEEYEAFINKEIETVVRFQEEIGLDVLVHGEPERNDMVQYFGE
QLNGFAFTTNGWVQSYGSRYVRPPIIVGDVSRPKAMTVKESVYAQSITSK
PMKGMLTGPVTILRWSFPRDDVSGKIQALQLGLALRDEVNDLEGAGITVI
QVDEPAIREGLPLRAGKERSDYLNWAAQSFRVATSGVENSTQIHSHFCYS
DLDPNHIKALDADVVSIEFSNYIQEFSEYPNHIGLGLFDIHSPRIPSKQE
FVSRIEEILKYPASKFWVNPDCGLKTRGWPEVKESLTNMVEAAKEFRAKY
Ligand information
Ligand IDC2F
InChIInChI=1S/C20H25N7O6/c1-27-12(9-23-16-15(27)18(31)26-20(21)25-16)8-22-11-4-2-10(3-5-11)17(30)24-13(19(32)33)6-7-14(28)29/h2-5,12-13,22H,6-9H2,1H3,(H,24,30)(H,28,29)(H,32,33)(H4,21,23,25,26,31)/t12-,13-/m0/s1
InChIKeyZNOVTXRBGFNYRX-STQMWFEESA-N
SMILES
SoftwareSMILES
CACTVS 3.341CN1[CH](CNc2ccc(cc2)C(=O)N[CH](CCC(O)=O)C(O)=O)CNC3=C1C(=O)NC(=N3)N
ACDLabs 10.04O=C(O)C(NC(=O)c1ccc(cc1)NCC2N(C=3C(=O)NC(=NC=3NC2)N)C)CCC(=O)O
OpenEye OEToolkits 1.5.0CN1C(CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)C(=O)NC(CCC(=O)O)C(=O)O
OpenEye OEToolkits 1.5.0C[N@@]1[C@H](CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)C(=O)N[C@@H](CCC(=O)O)C(=O)O
CACTVS 3.341CN1[C@@H](CNc2ccc(cc2)C(=O)N[C@@H](CCC(O)=O)C(O)=O)CNC3=C1C(=O)NC(=N3)N
FormulaC20 H25 N7 O6
Name5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID
ChEMBLCHEMBL1231574
DrugBankDB11256
ZINCZINC000002005305
PDB chain4l65 Chain A Residue 802 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4l65 Structural analysis of a fungal methionine synthase with substrates and inhibitors.
Resolution2.31 Å
Binding residue
(original residue number in PDB)		K19 N126 D504 Y527 R530 Y531 V532 W576
Binding residue
(residue number reindexed from 1)		K19 N115 D493 Y516 R519 Y520 V521 W565
Annotation score3
Enzymatic activity
Enzyme Commision number 2.1.1.14: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase.
Gene Ontology
Molecular Function
GO:0003871 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
GO:0008168 methyltransferase activity
GO:0008172 S-methyltransferase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006555 methionine metabolic process
GO:0006696 ergosterol biosynthetic process
GO:0008652 amino acid biosynthetic process
GO:0009086 methionine biosynthetic process
GO:0019280 L-methionine biosynthetic process from homoserine via O-acetyl-L-homoserine and cystathionine
GO:0032259 methylation
GO:0034605 cellular response to heat
GO:0052553 symbiont-mediated perturbation of host immune response
GO:0071266 'de novo' L-methionine biosynthetic process
Cellular Component
GO:0005634 nucleus
GO:0009277 fungal-type cell wall
GO:0009986 cell surface
GO:0030446 hyphal cell wall
GO:0062040 fungal biofilm matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4l65, PDBe:4l65, PDBj:4l65
PDBsum4l65
PubMed24524835
UniProtP82610|METE_CANAL 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (Gene Name=MET6)

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