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2X8F

Native structure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis

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 Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 1471
ChainResidue
ATRP93
AARG125
AMET151
AGLU152
AHOH2278

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1472
ChainResidue
AHOH2105
AHOH2144
AHOH2194
AHIS318
AHOH2009
AHOH2012
AHOH2104

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1473
ChainResidue
AASN406
ALYS407
AASN408

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1474
ChainResidue
AASP103
AVAL104
ATHR105
AHOH2015
AHOH2016

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1475
ChainResidue
AVAL73
ATYR84
AHOH2058
AHOH2059
AHOH2222

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1476
ChainResidue
AASN135
AILE136
AGLU137

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1477
ChainResidue
APHE48
AASP324
ATYR367

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1478
ChainResidue
ATHR311
AGLY312
ATYR313
APHE338
AARG348
AARG366
AHOH2269
AHOH2279

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1479
ChainResidue
ASER123
APRO124
ATYR189
AHOH2138
AHOH2280
AHOH2281

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 1480
ChainResidue
AHIS37
AHIS54
ALEU246
AARG337

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS B 1471
ChainResidue
BHIS37
BASP38
BTRP100
BVAL170
BASP171
BGLU224
BLEU246
BHIS318
BMRD1481
BHOH2013
BHOH2300

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 1472
ChainResidue
BTRP93
BARG125
BMET151
BGLU152
BHOH2301

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 1473
ChainResidue
BHIS318
BHOH2012
BHOH2014
BHOH2016
BHOH2105
BHOH2148
BHOH2203

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 1474
ChainResidue
BASP103
BVAL104
BTHR105
BHOH2018
BHOH2036

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 1475
ChainResidue
BVAL73
BTYR84
BHOH2060
BHOH2061
BHOH2241

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1476
ChainResidue
BTHR311
BGLY312
BTYR313
BARG348
BARG366
BHOH2200
BHOH2291
BHOH2302

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1477
ChainResidue
BLYS434
BLYS435
BASN459
BTHR460
BSER461

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1478
ChainResidue
BHOH2280
BHOH2303
BPHE353
BMET354
BLEU372
BHOH2209

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1479
ChainResidue
BASP324
BTYR367
BHOH2304

site_idCC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 1480
ChainResidue
BGLU43
BTHR44
BASN45
BGLN106
BGLY413
BGLU414
BMET415
BTHR416
BHOH2305
BHOH2306

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MRD B 1481
ChainResidue
BHIS37
BHIS54
BARG337
BTRS1471

Functional Information from PROSITE/UniProt
site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. ILEMNPKT
ChainResidueDetails
AILE195-THR202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:20883454
ChainResidueDetails
BASP38
AASP38

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:20883454
ChainResidueDetails
AGLU224
BGLU224

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN168
BASP38
BASP122
BASN168
AASP38
AASP122

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:20883454
ChainResidueDetails
ASER188
BSER188

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20883454
ChainResidueDetails
AHIS220
BHIS220

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AHIS318
BHIS318

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000305|PubMed:20883454
ChainResidueDetails
AASP171
BASP171

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Important for substrate recognition
ChainResidueDetails
AHIS318
BHIS318

219140

PDB entries from 2024-05-01

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