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1W32

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
AHOH2385
AHOH2405

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA B1347
ChainResidue
BASN258
BASN261
BASN262
BHOH2381
BHOH2389
BHOH2398
BASN253
BASP256

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1348
ChainResidue
ASER86
AASP137
AARG139
AARG152
AHOH2170
AHOH2508
AHOH2509

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A1349
ChainResidue
AARG299

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B1348
ChainResidue
BPHE130
BASP131
BSER132
BALA188
BHOH2508

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B1349
ChainResidue
BASP137
BARG139
BARG146
BGLN147
BHOH2252
BHOH2509
BHOH2510
BHOH2511

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B1350
ChainResidue
BALA270
BVAL271
BLEU276
BASN328
BHOH2417
BHOH2512

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B1351
ChainResidue
BARG168
BHOH2514
BHOH2515
BHOH2516

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B1352
ChainResidue
BTHR25
BSER26
BSER27
BALA28
BARG29
BHOH2045
BHOH2140
BHOH2517

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B1353
ChainResidue
BGLY1
BSER4
BTYR337
BHOH2495
BHOH2518

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B1354
ChainResidue
ATYR52
AGLY54
APRO90
AASN91
ATRP92
BHOH2391
BHOH2519

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 2024-08-21

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