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1OC6

structure native of the D405N mutant of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS at 1.5 angstrom resolution

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. VvYdlPdRDCAaaASnG
ChainResidueDetails
AVAL172-GLY188

site_idPS00656
Number of Residues10
DetailsGLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. ILVIEPDSLA
ChainResidueDetails
AILE220-ALA229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10057, ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12842048
ChainResidueDetails
AASP226

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10056, ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048
ChainResidueDetails
AASN405

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048
ChainResidueDetails
ATRP137
AASP139
AHIS271
ATRP274
AASN310
ATRP371
ALYS399
AGLU403

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (Man...) threonine => ECO:0000269|PubMed:9882628
ChainResidueDetails
ATHR118

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:9882628
ChainResidueDetails
ASER127

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048, ECO:0000269|PubMed:9882628
ChainResidueDetails
AASN141

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qk2
ChainResidueDetails
AARG179
AASP226
AASP180
ATYR174

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qk2
ChainResidueDetails
AASP226
AASN405

224572

PDB entries from 2024-09-04

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