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2UWF

Crystal structure of family 10 xylanase from Bacillus halodurans

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
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 1367
ChainResidue
AASP298
AGLU302
AHIS362
AHIS366

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1368
ChainResidue
AHOH2206
AHOH2208
AASP298
AARG357
AASP360
AHOH2169
AHOH2204

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1369
ChainResidue
AGLN28
ASER308
AILE311
AHOH2013
AHOH2015
AHOH2180

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1370
ChainResidue
AASP30
AGLU91
AHIS365
AHOH2077

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1371
ChainResidue
ATYR282
AASP321
AASP327
AASP340

Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. GLDNqVTELDM
ChainResidueDetails
AGLY258-MET268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU159

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10061
ChainResidueDetails
AGLU265

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AHIS236
AGLU265
AGLU159
AASP267

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AGLU159

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PDB entries from 2024-08-21

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