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1QNQ

The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10666621
ChainResidueDetails
AGLU169

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:10666621
ChainResidueDetails
AGLU276

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:10666621, ECO:0007744|PDB:1QNR
ChainResidueDetails
AGLU169
AGLU205
ATRP247

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for transglycosylation activity => ECO:0000269|DOI:10.3109/10242422.2012.674726
ChainResidueDetails
AARG171

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10666621, ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP, ECO:0007744|PDB:1QNQ
ChainResidueDetails
AASN130
AASN157
AASN250
AASN328

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
ATYR243
AGLU276
AGLU169
AHIS241
AASN168

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AARG54
AGLU276
AGLU169

227561

PDB entries from 2024-11-20

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