Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3CBH

THREE-DIMENSIONAL STRUCTURE OF CELLOBIOHYDROLASE FROM TRICHODERMA REESEI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030245biological_processcellulose catabolic process
Functional Information from PROSITE/UniProt
site_idPS00655
Number of Residues17
DetailsGLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAalASnG
ChainResidueDetails
AVAL167-GLY183

site_idPS00656
Number of Residues10
DetailsGLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. LLVIEPDSLA
ChainResidueDetails
ALEU215-ALA224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues364
DetailsRegion: {"description":"Catalytic","evidences":[{"source":"PubMed","id":"2377893","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12188666","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer that also modulates the pKa of Asp-245 and may act as a proton acceptor through a water chain","evidences":[{"source":"PubMed","id":"2377893","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"12188666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8875646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"12188666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8875646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"12188666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8875646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"12188666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8875646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qk2
ChainResidueDetails
AASP175
AASP221
ATYR169
AARG174

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qk2
ChainResidueDetails
AASP221
AASP401

site_idMCSA1
Number of Residues6
DetailsM-CSA 440
ChainResidueDetails
ATYR169modifies pKa, steric role
AARG174electrostatic stabiliser
AASP175modifies pKa, proton shuttle (general acid/base), transition state stabiliser
ASER181electrostatic stabiliser
AASP221proton shuttle (general acid/base)
AASP401electrostatic stabiliser

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon