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6TPP

Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033951molecular_functionoligosaccharide reducing-end xylanase activity
A0045493biological_processxylan catabolic process
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
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
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:27316951
ChainResidueDetails
AALA70
BALA70

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:27316951
ChainResidueDetails
AASP265
BASP265

223532

PDB entries from 2024-08-07

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