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2DRR

Crystal structure of reducing-end-xylose releasing exo-oligoxylanase D263N mutant

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
A0033951molecular_functionoligosaccharide reducing-end xylanase activity
A0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 1400
ChainResidue
AGLU27
AGLU30
AASP253
AHIS259

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1401
ChainResidue
AHOH1575
AHOH1671
AHOH1734
AGLU243
AGLY256
ATYR257
APHE261
AARG305

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1402
ChainResidue
ATRP36
AGLU37
AGLY41
AARG84
AHOH1729

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1403
ChainResidue
ATRP123
AGLU192
ATYR246
ATYR247
AASP248
AHOH1665
AHOH1892

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"A0A0S2UQQ5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"A0A0S2UQQ5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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