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4IPM

Crystal structure of a GH7 family cellobiohydrolase from Limnoria quadripunctata in complex with thiocellobiose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0016162molecular_functioncellulose 1,4-beta-cellobiosidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. GTVDSGSTLTVI
ChainResidueDetails
AGLY298-ILE309

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P62694
ChainResidueDetails
AGLU233

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P62694
ChainResidueDetails
AGLU238

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAQ
ChainResidueDetails
ATYR102
AASP124
ALYS202

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAP, ECO:0007744|PDB:4IPM
ChainResidueDetails
AASP235
AHIS249
ATRP401

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAQ, ECO:0007744|PDB:4IPM
ChainResidueDetails
AARG271

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAP, ECO:0007744|PDB:4HAQ, ECO:0007744|PDB:4IPM
ChainResidueDetails
AASP279
AARG417

218853

PDB entries from 2024-04-24

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