Structure of PDB 1auk Chain A Binding Site BS01

Receptor Information
>1auk Chain A (length=481) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSL
GTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLT
GMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPC
DGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRP
FFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDL
GLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFW
PGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKS
PRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASS
SLTAHEPPLLYDLSKDPGENYNLLGATPEVLQALKQLQLLKAQLDAAVTF
GPSQVARGEDPALQICCHPGCTPRPACCHCP
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1auk Chain A Residue 603 [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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PDB1auk Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		D29 D30 D281 N282
Binding residue
(residue number reindexed from 1)		D11 D12 D263 N264
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D29 D30 G69 R73 K123 H125 S150 H229 D281 N282 K302
Catalytic site (residue number reindexed from 1) D11 D12 G51 R55 K105 H107 S132 H211 D263 N264 K284
Enzyme Commision number 3.1.6.8: cerebroside-sulfatase.
Gene Ontology
Molecular Function
GO:0004065 arylsulfatase activity
GO:0004098 cerebroside-sulfatase activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008484 sulfuric ester hydrolase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006629 lipid metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005764 lysosome
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0035578 azurophil granule lumen
GO:0043202 lysosomal lumen
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:1auk, PDBe:1auk, PDBj:1auk
PDBsum1auk
PubMed9521684
UniProtP15289|ARSA_HUMAN Arylsulfatase A (Gene Name=ARSA)

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