Structure of PDB 3igu Chain A Binding Site BS01

Receptor Information
>3igu Chain A (length=387) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LDNGLLQTPPMGWLAWERFRCNINCDEDPKNCISEQLFMEMADRMAQDGW
RDMGYTYLNIDDCWIGGRDASGRLMPDPKRFPHGIPFLADYVHSLGLKLG
IYADMGNFTCMGYPGTTLDKVVQDAQTFAEWKVDMLKLDGCFSTPEERAQ
GYPKMAAALNATGRPIAFSCSWPAYEGGLPPRVQYSLLADICNLWRNYDD
IQDSWWSVLSILNWFVEHQDILQPVAGPGHWNDPDMLLIGNFGLSLEQSR
AQMALWTVLAAPLLMSTDLRTISAQNMDILQNPLMIKINQDPLGIQGRRI
HKEKSLIEVYMRPLSNKASALVFFSCRTDMPYRYHSSLGQLNFTGSVIYE
AQDVYSGDIISGLRDETNFTVIINPSGVVMWYLYPIK
Ligand information
Ligand ID7JZ
InChIInChI=1S/C6H10F2O5/c7-6(8)4(11)3(10)2(1-9)13-5(6)12/h2-5,9-12H,1H2/t2-,3+,4+,5-/m1/s1
InChIKeySHBCJQOMZTUYEL-MGCNEYSASA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC[CH]1O[CH](O)C(F)(F)[CH](O)[CH]1O
ACDLabs 10.04FC1(F)C(O)C(O)C(OC1O)CO
OpenEye OEToolkits 1.5.0C([C@@H]1[C@@H]([C@@H](C([C@@H](O1)O)(F)F)O)O)O
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)(F)F)O)O)O
CACTVS 3.341OC[C@H]1O[C@@H](O)C(F)(F)[C@@H](O)[C@H]1O
FormulaC6 H10 F2 O5
Name2-deoxy-2,2-difluoro-beta-D-lyxo-hexopyranose;
2-DEOXY-2,2-DIFLUORO-BETA-D-GALACTOPYRANOSYL-ENZYME INTERMEDIATE;
2-deoxy-2,2-difluoro-beta-D-lyxo-hexose;
2-deoxy-2,2-difluoro-D-lyxo-hexose;
2-deoxy-2,2-difluoro-lyxo-hexose
ChEMBL
DrugBank
ZINCZINC000005829825
PDB chain3igu Chain A Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3igu The 1.9 a structure of human alpha-N-acetylgalactosaminidase: The molecular basis of Schindler and Kanzaki diseases
Resolution2.15 Å
Binding residue
(original residue number in PDB)		W33 D78 D79 Y119 C127 K154 D156 D217
Binding residue
(residue number reindexed from 1)		W16 D61 D62 Y102 C110 K137 D139 D200
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D156 D217
Catalytic site (residue number reindexed from 1) D139 D200
Enzyme Commision number 3.2.1.49: alpha-N-acetylgalactosaminidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004557 alpha-galactosidase activity
GO:0008456 alpha-N-acetylgalactosaminidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0042803 protein homodimerization activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006629 lipid metabolic process
GO:0009311 oligosaccharide metabolic process
GO:0016052 carbohydrate catabolic process
GO:0016139 glycoside catabolic process
GO:0019377 glycolipid catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3igu, PDBe:3igu, PDBj:3igu
PDBsum3igu
PubMed19683538
UniProtP17050|NAGAB_HUMAN Alpha-N-acetylgalactosaminidase (Gene Name=NAGA)

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