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1WD4

Crystal structure of arabinofuranosidase complexed with arabinose

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019566biological_processarabinose metabolic process
A0031221biological_processarabinan metabolic process
A0031222biological_processarabinan catabolic process
A0045490biological_processpectin catabolic process
A0045493biological_processxylan catabolic process
A0046373biological_processL-arabinose metabolic process
A0046556molecular_functionalpha-L-arabinofuranosidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15292273
ChainResidueDetails
AGLU221

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:15292273
ChainResidueDetails
AASP297

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
ChainResidueDetails
AASP219
AGLU465
ALEU468
AASP488
AASN222
AASN223
AGLY296
AHIS416
AASN418
APHE419
AASP435
AHIS463

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cis-peptide bond => ECO:0000269|PubMed:15292273
ChainResidueDetails
ACYS176

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN83

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15292273
ChainResidueDetails
AASN202

226707

PDB entries from 2024-10-30

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