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1W2V

The 3-dimensional structure of a thermostable mutant of a xylanase (Xyn10A) from Cellvibrio japonicus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A1347
ChainResidue
AASN253
AASP256
AASN258
AASN261
AGLU262
AHOH2265
AHOH2266

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA B1347
ChainResidue
BASN258
BASN261
BGLU262
BHOH2267
BHOH2280
BHOH2282
BASN253
BASP256

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B1348
ChainResidue
ATYR52
AGLY54
APRO90
AASN91
ATRP92
BHOH2375
BHOH2376

Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. TLKIkITELDV
ChainResidueDetails
ATHR239-VAL249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU127
BGLU127

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AGLU246
BGLU246

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AHIS215
AASP248
AGLU246
AGLU127

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
BHIS215
BASP248
BGLU246
BGLU127

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AGLU127

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
BGLU127

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PDB entries from 2024-11-06

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