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5H4U

Crystal structure of cellulase from Antarctic springtail, Cryptopygus antarcticus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0008810molecular_functioncellulase activity
B0005975biological_processcarbohydrate metabolic process
B0008810molecular_functioncellulase activity
C0005975biological_processcarbohydrate metabolic process
C0008810molecular_functioncellulase activity
Functional Information from PROSITE/UniProt
site_idPS01140
Number of Residues12
DetailsGLYCOSYL_HYDROL_F45 Glycosyl hydrolases family 45 active site. TTRYWDcckpsC
ChainResidueDetails
ATHR8-CYS19

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10069, ECO:0000305|PubMed:28156112
ChainResidueDetails
AASP13
BASP13
CASP13

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:28156112
ChainResidueDetails
AASP122
BASP122
CASP122

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN39
BASN39
CASN39

222926

PDB entries from 2024-07-24

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