Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6KKA

Xylanase J mutant from Bacillus sp. 41M-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 401
ChainResidue
AGLU213
AGLU215
AASN232
AASP322

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 402
ChainResidue
ATYR237
AASP313
ATRP317
AASP318
AHOH519

site_idAC3
Number of Residues4
Detailsbinding site for residue CA A 403
ChainResidue
AASN44
AGLU183
AHOH505
AHOH620

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 404
ChainResidue
AGLN186
AHOH512
AHOH572
AHOH585
AHOH623

site_idAC5
Number of Residues7
Detailsbinding site for residue EPE A 405
ChainResidue
AARG269
AASP271
AASN278
ATHR281
ATHR311
AALA312
AHOH544

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 406
ChainResidue
ALYS19
AGLY23
AHOH562
AHOH571
BASN41

site_idAC7
Number of Residues2
Detailsbinding site for residue GOL A 407
ChainResidue
AGLY12
ALYS51

site_idAC8
Number of Residues2
Detailsbinding site for residue GOL A 408
ChainResidue
ASER24
AGLY25

site_idAC9
Number of Residues3
Detailsbinding site for residue GOL A 409
ChainResidue
AASN78
ATHR228
AASN232

site_idAD1
Number of Residues6
Detailsbinding site for residue MPD A 410
ChainResidue
AGLU16
ATRP18
AARG48
ATYR84
ATRP86
AILE134

site_idAD2
Number of Residues5
Detailsbinding site for residue MPD A 412
ChainResidue
ATYR80
AARG128
AGLN142
ATRP144
AHOH529

site_idAD3
Number of Residues4
Detailsbinding site for residue CA B 401
ChainResidue
BGLU213
BGLU215
BASN232
BASP322

site_idAD4
Number of Residues5
Detailsbinding site for residue CA B 402
ChainResidue
BTYR237
BASP313
BTRP317
BASP318
BHOH541

site_idAD5
Number of Residues4
Detailsbinding site for residue CA B 403
ChainResidue
BASN44
BGLU183
BHOH552
BHOH565

site_idAD6
Number of Residues6
Detailsbinding site for residue EPE B 404
ChainResidue
BARG269
BASP271
BASN278
BTHR311
BGOL409
BHOH548

site_idAD7
Number of Residues7
Detailsbinding site for residue CIT B 405
ChainResidue
BTYR80
BARG128
BGLN142
BGLU183
BTYR185
BSER229
BHOH565

site_idAD8
Number of Residues3
Detailsbinding site for residue GOL B 406
ChainResidue
BGLU16
BARG48
BTYR84

site_idAD9
Number of Residues2
Detailsbinding site for residue GOL B 407
ChainResidue
BASN78
BASN232

site_idAE1
Number of Residues4
Detailsbinding site for residue GOL B 408
ChainResidue
BSER24
BGLN38
BTRP39
BSER40

site_idAE2
Number of Residues4
Detailsbinding site for residue GOL B 409
ChainResidue
AGLY302
AASN303
BTHR311
BEPE404

site_idAE3
Number of Residues3
Detailsbinding site for residue GOL B 410
ChainResidue
BASN266
BHOH521
BHOH584

site_idAE4
Number of Residues5
Detailsbinding site for residue MPD B 411
ChainResidue
AGLY23
ASER40
BGLY23
BSER24
BSER40

site_idAE5
Number of Residues6
Detailsbinding site for residue MPD B 412
ChainResidue
BTYR13
BLEU198
AASP11
AGLY12
AHOH550
BGLY12

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon