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2DCJ

A two-domain structure of alkaliphilic XynJ from Bacillus sp. 41M-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030246molecular_functioncarbohydrate binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AGLU213
AGLU215
AASN232
AASP322
AHOH3145

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1002
ChainResidue
BGOL3012
BHOH3377
BGLU213
BGLU215
BASN232
BASP322

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
ATYR237
AASP313
ATRP317
AASP318
AHOH3159
AHOH3425

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1004
ChainResidue
BTYR237
BASP313
BTRP317
BASP318
BHOH3059
BHOH3190

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD A 2001
ChainResidue
AGLU16
ATRP18
AARG48
ATYR84
ATRP86
ASER133
AILE134
AHOH3065

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD B 2002
ChainResidue
BGLU16
BTRP18
BARG48
BTYR84
BTRP86
BSER133
BILE134
BHOH3022

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 2003
ChainResidue
AGLY12
ATYR13
ALEU198
AHOH3239

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD B 2004
ChainResidue
AASP11
AGLY12
BGLY12
BLEU198
BILE200
BHOH3430

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 3001
ChainResidue
BILE200
BSER254
BSER255
BASN295
BARG327
BHOH3102

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 3002
ChainResidue
AASN266
AHOH3156
AHOH3232
AHOH3411
BASN264
BASN266

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 3003
ChainResidue
BASN68
BSER195

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 3004
ChainResidue
AGLY23
AASN41
AASN43
AHOH3025
AHOH3180
AHOH3181
AHOH3429

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 3005
ChainResidue
APHE231
AASN232
AARG259
AASP322
ATYR323
AHOH3251

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 3006
ChainResidue
AASN263
AASN264
AGLY315
ATHR316
ATRP317
AASP318
AGOL3007
AHOH3425

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 3007
ChainResidue
AGOL3006
AHOH3375

site_idBC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 3009
ChainResidue
ASER4
AASN5
ALYS19
AASP20
AHOH3026
AHOH3036
AHOH3106
AHOH3209
AHOH3430
BALA290

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 3010
ChainResidue
BLYS19
BASP20
BHOH3049
BHOH3063
BHOH3191
BHOH3193
AHOH3207
BSER4
BASN5

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 3011
ChainResidue
ATYR80
APRO106
AGLN142
ATRP144
AHOH3332
AHOH3385
AHOH3446
AHOH3447

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 3012
ChainResidue
BARG259
BASP322
BCA1002
BHOH3112
BHOH3113
BHOH3377

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEFYIVDsW
ChainResidueDetails
APRO90-TRP100

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. LtvEGYQSSGsA
ChainResidueDetails
ALEU180-ALA191

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
AGLU183
AGLU93

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
BGLU183
BGLU93

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PDB entries from 2024-07-24

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