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3KL0

Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004348molecular_functionglucosylceramidase activity
A0005576cellular_componentextracellular region
A0006665biological_processsphingolipid metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033940molecular_functionglucuronoarabinoxylan endo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
B0004348molecular_functionglucosylceramidase activity
B0005576cellular_componentextracellular region
B0006665biological_processsphingolipid metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033940molecular_functionglucuronoarabinoxylan endo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
C0004348molecular_functionglucosylceramidase activity
C0005576cellular_componentextracellular region
C0006665biological_processsphingolipid metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0033940molecular_functionglucuronoarabinoxylan endo-1,4-beta-xylanase activity
C0045493biological_processxylan catabolic process
D0004348molecular_functionglucosylceramidase activity
D0005576cellular_componentextracellular region
D0006665biological_processsphingolipid metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0033940molecular_functionglucuronoarabinoxylan endo-1,4-beta-xylanase activity
D0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLA A 402
ChainResidue
ATRP268
ATYR269
AARG272
ATYR274
AHIS405
AHIS406
AHOH614
AHOH840
AHOH1759

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLA A 403
ChainResidue
AARG353
ATHR366
AHIS378
AHOH446
AHOH728
AHOH753
CASN338

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TAR A 404
ChainResidue
ALYS13
AARG303
AASP305
AALA306
AHOH416
AHOH591
AHOH1072
BLYS126

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HIS A 405
ChainResidue
AGLU140
ATYR143
ATYR204
ATYR231
AMLA402
AHIS406
AHOH840
AHOH1544
AHOH1648

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HIS A 406
ChainResidue
ATYR204
AGLU229
ATRP268
AMLA402
AHIS405
AHOH1527
AHOH1544
AHOH1859

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 407
ChainResidue
AHOH490
AHOH541
AHOH556
AHOH950
AHOH952
CHOH481

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MLA B 402
ChainResidue
AHIS398
BTRP268
BTYR269
BARG272
BTYR274
BHOH423
BHOH477
BHOH1740

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 403
ChainResidue
AHOH552
BHOH426
BHOH484
BHOH563
BHOH955
BHOH2148

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLA C 402
ChainResidue
BHIS395
BHIS396
CTRP268
CTYR269
CARG272
CTYR274
CHOH1359
CHOH1371
CHOH1693
DHOH494

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA C 403
ChainResidue
CHOH424
CHOH457
CHOH1099
CHOH1111
CHOH2157

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLA D 402
ChainResidue
CHOH2086
DTRP268
DTYR269
DARG272
DTYR274
DHOH435
DHOH1756

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA D 403
ChainResidue
DHOH432
DHOH499
DHOH834
DHOH880
DHOH887

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:21256135
ChainResidueDetails
AGLU140
BGLU140
CGLU140
DGLU140

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:21256135
ChainResidueDetails
AGLU229
BGLU229
CGLU229
DGLU229

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PDB entries from 2024-07-24

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