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1PT2

Crystal structure of levansucrase (E342A) complexed with sucrose

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0009758biological_processcarbohydrate utilization
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0046872molecular_functionmetal ion binding
A0050053molecular_functionlevansucrase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:14517548
ChainResidueDetails
AASP86

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:14517548
ChainResidueDetails
AALA342

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:14517548, ECO:0007744|PDB:1PT2, ECO:0007744|PDB:3BYN
ChainResidueDetails
ATRP85
AASP86
ASER164
AARG246
AASP247
AGLU340
AARG360

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:14517548, ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, ECO:0000269|PubMed:33303628, ECO:0007744|PDB:1OYG, ECO:0007744|PDB:1PT2, ECO:0007744|PDB:2VDT, ECO:0007744|PDB:3BYJ, ECO:0007744|PDB:3BYK, ECO:0007744|PDB:3BYN, ECO:0007744|PDB:6PWQ, ECO:0007744|PDB:6VHQ
ChainResidueDetails
AASP241
AGLN272
ALEU308
AASN310
AASP339

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:14517548
ChainResidueDetails
AASP247

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 875
ChainResidueDetails
AASP86covalent catalysis
ASER164steric locator
AASP247electrostatic stabiliser
AALA342proton shuttle (general acid/base)

218853

PDB entries from 2024-04-24

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