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2PP1

Crystal structure of L-talarate/galactarate dehydratase from Salmonella typhimurium LT2 liganded with Mg and L-lyxarohydroxamate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008867molecular_functiongalactarate dehydratase activity
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0046392biological_processgalactarate catabolic process
A0046872molecular_functionmetal ion binding
A1903663biological_processL-altrarate catabolic process
A1990594molecular_functionL-altrarate dehydratase activity
B0000287molecular_functionmagnesium ion binding
B0008867molecular_functiongalactarate dehydratase activity
B0009063biological_processamino acid catabolic process
B0016052biological_processcarbohydrate catabolic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0046392biological_processgalactarate catabolic process
B0046872molecular_functionmetal ion binding
B1903663biological_processL-altrarate catabolic process
B1990594molecular_functionL-altrarate dehydratase activity
C0000287molecular_functionmagnesium ion binding
C0008867molecular_functiongalactarate dehydratase activity
C0009063biological_processamino acid catabolic process
C0016052biological_processcarbohydrate catabolic process
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
C0046392biological_processgalactarate catabolic process
C0046872molecular_functionmetal ion binding
C1903663biological_processL-altrarate catabolic process
C1990594molecular_functionL-altrarate dehydratase activity
D0000287molecular_functionmagnesium ion binding
D0008867molecular_functiongalactarate dehydratase activity
D0009063biological_processamino acid catabolic process
D0016052biological_processcarbohydrate catabolic process
D0016829molecular_functionlyase activity
D0016836molecular_functionhydro-lyase activity
D0046392biological_processgalactarate catabolic process
D0046872molecular_functionmetal ion binding
D1903663biological_processL-altrarate catabolic process
D1990594molecular_functionL-altrarate dehydratase activity
E0000287molecular_functionmagnesium ion binding
E0008867molecular_functiongalactarate dehydratase activity
E0009063biological_processamino acid catabolic process
E0016052biological_processcarbohydrate catabolic process
E0016829molecular_functionlyase activity
E0016836molecular_functionhydro-lyase activity
E0046392biological_processgalactarate catabolic process
E0046872molecular_functionmetal ion binding
E1903663biological_processL-altrarate catabolic process
E1990594molecular_functionL-altrarate dehydratase activity
F0000287molecular_functionmagnesium ion binding
F0008867molecular_functiongalactarate dehydratase activity
F0009063biological_processamino acid catabolic process
F0016052biological_processcarbohydrate catabolic process
F0016829molecular_functionlyase activity
F0016836molecular_functionhydro-lyase activity
F0046392biological_processgalactarate catabolic process
F0046872molecular_functionmetal ion binding
F1903663biological_processL-altrarate catabolic process
F1990594molecular_functionL-altrarate dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 399
ChainResidue
ALYS195
AASP226
AGLU252
AGLU278
ALLH801
AHOH944

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 444
ChainResidue
BGLU278
BLLH802
BHOH939
BLYS195
BASP226
BGLU252

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE LLH A 801
ChainResidue
AASP46
ALYS48
ALYS82
AARG83
APHE171
ALYS195
ALYS197
AASP226
AASN228
AGLU278
AHIS328
AGLU348
ATRP352
AMG399
AHOH811
AHOH938
AHOH939

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE LLH B 802
ChainResidue
BASP46
BLYS48
BLYS82
BARG83
BPHE171
BLYS195
BLYS197
BASP226
BASN228
BGLU278
BHIS328
BGLU348
BTRP352
BMG444
BHOH814
BHOH931
BHOH937

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE LLH C 803
ChainResidue
CASP46
CLYS48
CLYS82
CARG83
CPHE171
CLYS195
CLYS197
CASP226
CASN228
CGLU278
CHIS328
CGLU348
CTRP352
CHOH818
CHOH855
CHOH868
CHOH874

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE LLH D 804
ChainResidue
DASP46
DLYS48
DLYS82
DARG83
DPHE171
DLYS195
DLYS197
DASP226
DASN228
DGLU278
DHIS328
DGLU348
DTRP352
DHOH827
DHOH834
DHOH862
DHOH869

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE LLH E 805
ChainResidue
EASP46
ELYS48
ELYS82
EARG83
EPHE171
ELYS195
ELYS197
EASP226
EASN228
EGLU252
EGLU278
EHIS328
EGLU348
ETRP352
EHOH819
EHOH880
EHOH891
EHOH895

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE LLH F 806
ChainResidue
FLYS48
FLYS82
FARG83
FPHE171
FLYS195
FLYS197
FASP226
FASN228
FGLU252
FGLU278
FHIS328
FGLU348
FTRP352
FHOH830
FHOH844
FHOH884
FHOH891
FASP46

Functional Information from PROSITE/UniProt
site_idPS00909
Number of Residues32
DetailsMR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LmvDaNqqwdretAirmgrkMeqfnliwIEEP
ChainResidueDetails
ALEU223-PRO254

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17649980","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17649980","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues54
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17649980","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Increases basicity of active site His"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
AHIS328
AGLU348
ALYS197
AASP301

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
DLYS195
DPRO355
DLYS197

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
ELYS195
EPRO355
ELYS197

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
FLYS195
FPRO355
FLYS197

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
BHIS328
BGLU348
BLYS197
BASP301

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
CHIS328
CGLU348
CLYS197
CASP301

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
DHIS328
DGLU348
DLYS197
DASP301

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
EHIS328
EGLU348
ELYS197
EASP301

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
FHIS328
FGLU348
FLYS197
FASP301

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
ALYS195
APRO355
ALYS197

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
BLYS195
BPRO355
BLYS197

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mdr
ChainResidueDetails
CLYS195
CPRO355
CLYS197

243083

PDB entries from 2025-10-15

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