Structure of PDB 1m2t Chain A Binding Site BS01

Receptor Information
>1m2t Chain A (length=248) Species: 3972 (Viscum album) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YERLRLRTDQQTTGAEYFSFITVLRDYVSSGSFSNNIPLLRQSTVPVSEG
QRFVLVELTNAGGDTITAAIDVTNLYVVAYEAGNQSYFLSDAPAGAETQD
FSGTTSSSQPFNGSYPDLERYAGHRDQIPLGIDQLIQSVTALRFPGGQTK
TQARSILILIQMISEAARFNPILWRARQYINSGASFLPDVYMLELETSWG
QQSTQVQHSTDGVFNNPIALAIAPGVIVTLTNIRDVIASLAIMLFVCG
Ligand information
Ligand IDADE
InChIInChI=1S/C5H5N5/c6-4-3-5(9-1-7-3)10-2-8-4/h1-2H,(H3,6,7,8,9,10)
InChIKeyGFFGJBXGBJISGV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ncnc2[nH]cnc12
OpenEye OEToolkits 1.5.0c1[nH]c2c(n1)c(ncn2)N
ACDLabs 10.04n1c(c2ncnc2nc1)N
FormulaC5 H5 N5
NameADENINE
ChEMBLCHEMBL226345
DrugBankDB00173
ZINCZINC000000000882
PDB chain1m2t Chain A Residue 9550 [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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PDB1m2t Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution.
Resolution1.89 Å
Binding residue
(original residue number in PDB)		Y76 V77 G113 Y115 I160 R168
Binding residue
(residue number reindexed from 1)		Y76 V77 G113 Y115 I160 R168
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) V77 E165 R168
Catalytic site (residue number reindexed from 1) V77 E165 R168
Enzyme Commision number 3.2.2.22: rRNA N-glycosylase.
Gene Ontology
Molecular Function
GO:0030598 rRNA N-glycosylase activity
Biological Process
GO:0017148 negative regulation of translation

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Molecular Function
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Biological Process
External links
PDB RCSB:1m2t, PDBe:1m2t, PDBj:1m2t
PDBsum1m2t
PubMed12351890
UniProtP81446|ML1_VISAL Beta-galactoside-specific lectin 1

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