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1BS9

ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0030245biological_processcellulose catabolic process
A0045493biological_processxylan catabolic process
A0046555molecular_functionacetylxylan esterase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 208
ChainResidue
ATHR146
AASP172
AALA173
ASER174
AHOH399

site_idCAT
Number of Residues3
DetailsTHESE THREE RESIDUES FORM THE CATALYTIC TRIAD
ChainResidue
ASER90
AASP175
AHIS187

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. IVLVGYSQGG
ChainResidueDetails
AILE84-GLY93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ASER90
AASP175
AHIS187

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN180

Catalytic Information from CSA
site_idCSA1
Number of Residues7
Detailsa catalytic site defined by CSA, PubMed 10089308
ChainResidueDetails
ATHR13
ATHR13
AASP175
ASER90
AHIS187
AGLN91
AGLN91

site_idMCSA1
Number of Residues5
DetailsM-CSA 431
ChainResidueDetails
ATHR13electrostatic stabiliser
ASER90covalent catalysis, proton shuttle (general acid/base)
AGLN91steric role
AASP175modifies pKa
AHIS187proton shuttle (general acid/base)

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PDB entries from 2024-10-30

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