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1QW9

Crystal structure of a family 51 alpha-L-arabinofuranosidase in complex with 4-nitrophenyl-Ara

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0005737cellular_componentcytoplasm
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031222biological_processarabinan catabolic process
A0046373biological_processL-arabinose metabolic process
A0046556molecular_functionalpha-L-arabinofuranosidase activity
B0000272biological_processpolysaccharide catabolic process
B0005737cellular_componentcytoplasm
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031222biological_processarabinan catabolic process
B0046373biological_processL-arabinose metabolic process
B0046556molecular_functionalpha-L-arabinofuranosidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:11943144, ECO:0000305|PubMed:12221104, ECO:0000305|PubMed:14517232
ChainResidueDetails
AMET176
BMET176

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12221104, ECO:0000305|PubMed:14517232
ChainResidueDetails
ATRP295
BTRP295

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:14517232, ECO:0007744|PDB:1PZ2, ECO:0007744|PDB:1QW8, ECO:0007744|PDB:1QW9
ChainResidueDetails
AHIS30
APHE75
ATYR247
BHIS30
BPHE75
BTYR247

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14517232, ECO:0007744|PDB:1PZ2, ECO:0007744|PDB:1QW9
ChainResidueDetails
AALA175
BALA175

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:14517232, ECO:0007744|PDB:1PZ2, ECO:0007744|PDB:1QW8, ECO:0007744|PDB:1QW9
ChainResidueDetails
ATRP295
BTRP295

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14517232, ECO:0007744|PDB:1QW8, ECO:0007744|PDB:1QW9
ChainResidueDetails
ALEU352
BLEU352

site_idSWS_FT_FI7
Number of Residues4
DetailsSITE: Important for substrate recognition => ECO:0000305|PubMed:14517232
ChainResidueDetails
ATYR299
ALEU352
BTYR299
BLEU352

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pz3
ChainResidueDetails
AALA175

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pz3
ChainResidueDetails
BALA175

site_idMCSA1
Number of Residues2
DetailsM-CSA 667
ChainResidueDetails
AMET176activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
ATRP295covalently attached, nucleofuge, nucleophile

site_idMCSA2
Number of Residues2
DetailsM-CSA 667
ChainResidueDetails
BMET176activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
BTRP295covalently attached, nucleofuge, nucleophile

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PDB entries from 2024-07-31

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