Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1PVX

DO-1,4-BETA-XYLANASE, ROOM TEMPERATURE, PH 4.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEYYIVEnF
ChainResidueDetails
APRO83-PHE93

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VatEGYFSSGyA
ChainResidueDetails
AVAL175-ALA186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062
ChainResidueDetails
AGLU86

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063
ChainResidueDetails
AGLU178

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylglycine => ECO:0000269|PubMed:10623548
ChainResidueDetails
AGLY1

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
AGLU86
AGLU178

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon