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3EMC

Crystal structure of XynB, an intracellular xylanase from Paenibacillus barcinonensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD A 500
ChainResidue
ATRP85
AGLU134
AGLN210
AHIS212
AGLU241
ATRP299
AHOH636
AHOH712

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD A 600
ChainResidue
AHIS212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU134

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AGLU241

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AHIS212
AASP243
AGLU134
AGLU241

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AGLU134

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PDB entries from 2024-08-14

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