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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4I5R

Crystal structure of a fungal chimeric cellobiohydrolase Cel6A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030245biological_processcellulose catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 501
ChainResidue
ALYS195
AASN198
AVAL208
AGLU209
ASER211
site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 A 502
ChainResidue
AASN102
AARG105
AHIS109
site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AGLU399
ALYS395
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AVAL193
ALYS197
AGLU245
AHOH767
site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
APRO321
APRO323
AHOH819
site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
ATRP99
AALA100
AARG105
AASN238
site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
ATHR229
AASN276
AHIS450
AHIS452
site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 508
ChainResidue
ALEU256
APRO257
AVAL259
AARG295
AALA296
AHOH729
AHOH765
Functional Information from PROSITE/UniProt
site_idPS00655
Number of Residues17
DetailsGLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAalASnG
ChainResidueDetails
AVAL168-GLY184
site_idPS00656
Number of Residues10
DetailsGLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. LLVIEPDSLA
ChainResidueDetails
ALEU216-ALA225
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10057","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
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_FI3
Number of Residues2
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_FI4
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_FI5
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_FI6
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
site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10056","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues22
DetailsRegion: {"description":"Substrate binding loop 1","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues38
DetailsRegion: {"description":"Substrate binding loop 2","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 440
ChainResidueDetails
ATYR170modifies pKa, steric role
AARG175electrostatic stabiliser
AASP176modifies pKa, proton shuttle (general acid/base), transition state stabiliser
ASER182electrostatic stabiliser
AASP222proton shuttle (general acid/base)
AASP401electrostatic stabiliser

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PDB entries from 2026-03-11

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