Structure of PDB 4e2z Chain A Binding Site BS03

Receptor Information
>4e2z Chain A (length=405) Species: 1874 (Micromonospora chalcea) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PTACRVCGGGVQEFLDLGRQPLSDRFRKPDELDDEFTYRLAVGRCDSCEM
VQLTEEVPRDLMFHEVYPYHSSGSSVMREHFAMLARDFLATELTGPDPFI
VEIGCNDGIMLRTIQEAGVRHLGFEPSSGVAAKAREKGIRVRTDFFEKAT
ADDVRRTEGPANVIYAANTLCHIPYVQSVLEGVDALLAPDGVFVFEDPYL
GDIVAKTSFDQIYDENFFLFSATSVQGMAQRCGFELVDVQRLPVHGGEVR
YTLARQGSRTPSAAVAQLLAAEREQELSDMATLRAFAGNVVKIRDELTAL
LHRLRAEGRSVVGYGATAKSATVTNFCGIGPDLVHSVYDTTPDKQNRLTP
GAHIPVRPASAFSDPYPDYALLFAWNHAEEIMAKEQEFHQAGGRWILYVP
EVHIR
Ligand information
Ligand IDJHZ
InChIInChI=1S/C17H27N3O13P2/c1-8-6-20(16(24)19-15(8)23)12-4-10(21)11(31-12)7-29-34(25,26)33-35(27,28)32-13-5-17(3,18)14(22)9(2)30-13/h6,9-13,21H,4-5,7,18H2,1-3H3,(H,25,26)(H,27,28)(H,19,23,24)/t9-,10+,11-,12-,13-,17+/m1/s1
InChIKeyLXNLHPYBLNFMEH-XXXNSVIPSA-N
SMILES
SoftwareSMILES
CACTVS 3.370C[CH]1O[CH](C[C](C)(N)C1=O)O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH](C[CH]2O)N3C=C(C)C(=O)NC3=O
CACTVS 3.370C[C@H]1O[C@@H](C[C@](C)(N)C1=O)O[P](O)(=O)O[P](O)(=O)OC[C@H]2O[C@H](C[C@@H]2O)N3C=C(C)C(=O)NC3=O
OpenEye OEToolkits 1.7.6CC1C(=O)C(CC(O1)OP(=O)(O)OP(=O)(O)OCC2C(CC(O2)N3C=C(C(=O)NC3=O)C)O)(C)N
OpenEye OEToolkits 1.7.6C[C@@H]1C(=O)[C@@](C[C@H](O1)OP(=O)(O)OP(=O)(O)OC[C@@H]2[C@H](C[C@@H](O2)N3C=C(C(=O)NC3=O)C)O)(C)N
ACDLabs 12.01O=C1C(=CN(C(=O)N1)C2OC(C(O)C2)COP(=O)(OP(=O)(OC3OC(C(=O)C(N)(C3)C)C)O)O)C
FormulaC17 H27 N3 O13 P2
Name
ChEMBL
DrugBank
ZINCZINC000008437097
PDB chain4e2z Chain A Residue 504 [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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PDB4e2z Probing the catalytic mechanism of a C-3'-methyltransferase involved in the biosynthesis of D-tetronitrose.
Resolution1.41 Å
Binding residue
(original residue number in PDB)		Y76 Y78 N177 Y222 E224 H254 T326 A327 K328 D348 T349 K353 N385 H386 E389 I390 K393
Binding residue
(residue number reindexed from 1)		Y67 Y69 N168 Y213 E215 H245 T317 A318 K319 D339 T340 K344 N376 H377 E380 I381 K384
Annotation score1
Enzymatic activity
Enzyme Commision number 2.1.1.-
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0032259 methylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4e2z, PDBe:4e2z, PDBj:4e2z
PDBsum4e2z
PubMed22495991
UniProtB5L6K6

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