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3C7E

Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0045493biological_processxylan catabolic process
A0046556molecular_functionalpha-L-arabinofuranosidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 488
ChainResidue
AGLU359
AGLU361
AASN383
AGLN384
AASP480

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 489
ChainResidue
AHOH2361
AARG368
ASER388
AGLN390
AASP393

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 490
ChainResidue
AHIS290
AHOH2067
AHOH2068
AHOH2128
AHOH2171
AHOH2184
AHOH2358

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 2055
ChainResidue
AASP219
APRO268
APHE269
AHOH2335

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 2056
ChainResidue
AGLY32
APHE296
ALYS297
AHOH2262

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 2057
ChainResidue
AASN342
ATYR343
AALA344

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 2058
ChainResidue
AASP24
ALEU59
AARG321
AHOH2322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:18980579
ChainResidueDetails
AASP24

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:18980579
ChainResidueDetails
AGLU225

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18980579
ChainResidueDetails
AASN288
AGLU359
AGLU361
AASN383
AGLN384
AASP480

site_idSWS_FT_FI4
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:18980579
ChainResidueDetails
AASP163

220113

PDB entries from 2024-05-22

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