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1GA2

THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030246molecular_functioncarbohydrate binding
A0030248molecular_functioncellulose binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0030246molecular_functioncarbohydrate binding
B0030248molecular_functioncellulose binding
Functional Information from PROSITE/UniProt
site_idPS00592
Number of Residues25
DetailsGH9_2 Glycosyl hydrolases family 9 (GH9) active site signature 2. YALGsTgr..SFVVGy....GvnPPqhPHHR
ChainResidueDetails
ATYR351-ARG375

site_idPS00698
Number of Residues19
DetailsGH9_3 Glycosyl hydrolases family 9 (GH9) active site signature 3. YtDeinnYvnnEiAcdyNA
ChainResidueDetails
ATYR409-ALA427

site_idPS60032
Number of Residues18
DetailsGH9_1 Glycosyl hydrolases family 9 (GH9) active site signature 1. LtGGWYDAGDhvKFnLPM
ChainResidueDetails
ALEU49-MET66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10140
ChainResidueDetails
AASP58
BASP58

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10059
ChainResidueDetails
AHIS373
BHIS373

site_idSWS_FT_FI3
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10060
ChainResidueDetails
AASP411
AGLU420
BASP411
BGLU420

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1js4
ChainResidueDetails
AASP58
AGLU420
AASP55

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1js4
ChainResidueDetails
BASP58
BGLU420
BASP55

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PDB entries from 2024-07-17

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