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3VZL

Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) N35H mutant

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
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0031176molecular_functionendo-1,4-beta-xylanase activity
C0045493biological_processxylan catabolic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0031176molecular_functionendo-1,4-beta-xylanase activity
D0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 201
ChainResidue
BTHR123
BTHR124
CSER100
CASP101
CASN148
CHOH357

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 201
ChainResidue
CTYR94
CGLY96
CTHR97

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 201
ChainResidue
DSER100
DASP101
DASN148
DHOH322
DHOH348

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

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS
ChainResidueDetails
AMET169-SER180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418
ChainResidueDetails
AGLU78
BGLU78
CGLU78
DGLU78

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418
ChainResidueDetails
AGLU172
BGLU172
CGLU172
DGLU172

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
AHIS35modifies pKa
ATYR69electrostatic destabiliser
AGLU78covalent catalysis, proton shuttle (general acid/base)
ATYR80modifies pKa
AGLU172proton shuttle (general acid/base)

site_idMCSA2
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
BHIS35modifies pKa
BTYR69electrostatic destabiliser
BGLU78covalent catalysis, proton shuttle (general acid/base)
BTYR80modifies pKa
BGLU172proton shuttle (general acid/base)

site_idMCSA3
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
CHIS35modifies pKa
CTYR69electrostatic destabiliser
CGLU78covalent catalysis, proton shuttle (general acid/base)
CTYR80modifies pKa
CGLU172proton shuttle (general acid/base)

site_idMCSA4
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
DHIS35modifies pKa
DTYR69electrostatic destabiliser
DGLU78covalent catalysis, proton shuttle (general acid/base)
DTYR80modifies pKa
DGLU172proton shuttle (general acid/base)

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PDB entries from 2024-07-17

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