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1WL7

Structure of the thermostable arabinanase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031222biological_processarabinan catabolic process
A0046558molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 314
ChainResidue
AHIS271
AHOH317
AHOH321
AHOH338
AHOH343
AHOH374
AHOH412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:15944411
ChainResidueDetails
AASP27

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:15944411
ChainResidueDetails
AGLU201

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP27
AASN144
ASER164

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLY105

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AHIS271

site_idSWS_FT_FI6
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:15944411
ChainResidueDetails
AASP147

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for substrate recognition => ECO:0000250
ChainResidueDetails
AHIS271

229380

PDB entries from 2024-12-25

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