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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
DetailsCARBOHYD: O-linked (Man...) threonine => ECO:0000269|PubMed:9882628
ChainResidueDetails
ATHR117

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:9882628
ChainResidueDetails
ASER126

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:12188666
ChainResidueDetails
AASP222

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer that also modulates the pKa of Asp-245 and may act as a proton acceptor through a water chain => ECO:0000269|PubMed:2377893
ChainResidueDetails
AASP176

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
ChainResidueDetails
AASN290

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 2024-07-10

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