Structure of PDB 1c8y Chain A Binding Site BS01

Receptor Information
>1c8y Chain A (length=265) Species: 1922 (Streptomyces plicatus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KQGPTSVAYVEVNNNSMLNVGKYTLADGGGNAFDVAVIFAANINYDTGTK
TAYLHFNENVQRVLDNAVTQIRPLQQQGIKVLLSVLGNHQGAGFANFPSQ
QAASAFAKQLSDAVAKYGLDGVDFADEYAEYGNNGTAQPNDSSFVHLVTA
LRANMPDKIISLYNIGPAASRLSYGGVDVSDKFDYAWNPYYGTWQVPGIA
LPKAQLSPAAVEIGRTSRSTVADLARRTVDEGYGVYLTYNLDGGDRTADV
SAFTRELYGSEAVRT
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1c8y Chain A Residue 271 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1c8y Mutations of endo-beta-N-acetylglucosaminidase H active site residues Asp130 and Glu132: activities and conformations.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		H94 E135
Binding residue
(residue number reindexed from 1)		H89 E130
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) A130 E132
Catalytic site (residue number reindexed from 1) A125 E127
Enzyme Commision number 3.2.1.96: mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033925 mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1c8y, PDBe:1c8y, PDBj:1c8y
PDBsum1c8y
PubMed10595536
UniProtP04067|EBAG_STRPL Endo-beta-N-acetylglucosaminidase H

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