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2Z79

High resolution crystal structure of a glycoside hydrolase family 11 xylanase of Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 186
ChainResidue
ATRP9
AVAL37
AGLU78
ATYR80
ATYR174
AGOL187
AGOL188
AHOH1755
AHOH1760

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 187
ChainResidue
ATYR65
AARG112
AGLN127
ATRP129
ATYR174
AGOL186

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 186
ChainResidue
BTYR65
BTYR80
BARG112
BGLN127
BGOL187
BHOH1886

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GOL B 187
ChainResidue
BTRP9
BVAL37
BGLU78
BTYR80
BARG112
BTYR174
BGOL186
BGOL188
BHOH1745
BHOH1900
BHOH1901
BHOH1904
BHOH1907

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 188
ChainResidue
BGLN7
BTRP9
BVAL37
BTYR69
BTYR166
BGOL187
BHOH1890
BHOH1900
BHOH1901

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 188
ChainResidue
AGLN7
ATRP9
AVAL37
ATYR69
ATYR166
AGOL186

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A1733
ChainResidue
AARG132
AARG136
APRO137
ASER140
AASN141
AHOH1746
AHOH1756
AHOH1795
AHOH1845
AHOH1900

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B1733
ChainResidue
ATYR113
BTHR3
BASP4
BTYR5
BASN20
BLYS40

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW
ChainResidueDetails
APRO75-TRP85

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:7911679
ChainResidueDetails
AGLU78
BGLU78

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063
ChainResidueDetails
AALA172
BALA172

219869

PDB entries from 2024-05-15

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