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1OYG

Crystal structure of Bacillus subtilis levansucrase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0009758biological_processcarbohydrate utilization
A0016757molecular_functionglycosyltransferase activity
A0046872molecular_functionmetal ion binding
A0050053molecular_functionlevansucrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 500
ChainResidue
AASP241
AGLN272
ALEU308
AASN310
AASP339
AHOH532

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 501
ChainResidue
AEDO502
AHOH584
AASP94
AALA151
AASN152

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
AASP94
AASN152
AGLU252
AASP253
ALYS348
AEDO501
AHOH525
AHOH578
AHOH850

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AHIS104
AGLN126
AGLY129
AGLU130
ATHR470
AASN472
AHOH572

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AASN242
AARG246
AGLU340
ALYS363

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AASN450
ALYS452
ALYS455
ATHR456
ASER457

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AGLN229
AALA419
ALYS420
AVAL471
AASN472
AHOH635
AHOH659
AHOH792
AHOH835

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
APHE169
AILE217
ATHR323
ALEU324
AHOH681
AHOH871

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
AGLU342

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_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 14517548
ChainResidueDetails
AGLU342
AASP86
AASP247

site_idMCSA1
Number of Residues4
DetailsM-CSA 875
ChainResidueDetails
AASP86covalent catalysis
ASER164steric locator
AASP247electrostatic stabiliser
AGLU342proton shuttle (general acid/base)

224201

PDB entries from 2024-08-28

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