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1W3H

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
AASN262
AHOH2251
AHOH2252

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B1348
ChainResidue
BASN258
BASN261
BASN262
BHOH2239
BHOH2248
BASN253
BASP256

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1348
ChainResidue
AHIS84
AASP134
AARG146
ASER148
AHOH2043
AHOH2307
AHOH2308

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B1349
ChainResidue
BHIS84
BASP134
BARG146
BSER148
BHOH2153
BHOH2319

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

224201

PDB entries from 2024-08-28

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