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1GYE

Structure of Cellvibrio cellulosa alpha-L-arabinanase complexed with Arabinohexaose

Functional Information from GO Data
ChainGOidnamespacecontents
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0008152biological_processmetabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031222biological_processarabinan catabolic process
B0046556molecular_functionalpha-L-arabinofuranosidase activity
B0046558molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:12198486
ChainResidueDetails
BASP38

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:12198486
ChainResidueDetails
BGLU221

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:12198486
ChainResidueDetails
BASP35
BASP90
BGLY115
BASN155
BSER175
BGLU221
BGLN316

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
BHIS291

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000305|PubMed:12198486
ChainResidueDetails
BALA158

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for substrate recognition and stabilization
ChainResidueDetails
BHIS291

218853

PDB entries from 2024-04-24

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