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6TPP

Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis.

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
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033951molecular_functionoligosaccharide reducing-end xylanase activity
B0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 401
ChainResidue
AARG68
AASP128
AARG268
AEDO402

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 402
ChainResidue
AASP61
AASP265
AEDO401

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO B 401
ChainResidue
BTYR197
BARG68
BASP128

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO B 402
ChainResidue
BSER264
BASP265
BHOH536

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27316951","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"27316951","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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