Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1TZZ

Crystal structure of the protein L1841, unknown member of enolase superfamily from Bradyrhizobium japonicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0047808molecular_functionD(-)-tartrate dehydratase activity
A0051260biological_processprotein homooligomerization
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
B0047808molecular_functionD(-)-tartrate dehydratase activity
B0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 3501
ChainResidue
AASP1216
AGLU1242
AGLU1268
AHOH3322
AHOH3323
AHOH3324

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 3502
ChainResidue
BHOH3002
BHOH3172
BHOH3321
BASP2216
BGLU2242
BGLU2268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: acceptor => ECO:0000269|PubMed:17144653
ChainResidueDetails
ALYS1187
BLYS2187

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17144653
ChainResidueDetails
AHIS1325
BHIS2325

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AASN1024
BASN2024
BASN2058
BLYS2105
BTYR2159
BLYS2185
BGLU2242
BGLU2268
BHIS2325
BGLU2344
AASN1058
ALYS1105
ATYR1159
ALYS1185
AGLU1242
AGLU1268
AHIS1325
AGLU1344

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17144653
ChainResidueDetails
AASP1216
BASP2216

site_idSWS_FT_FI5
Number of Residues6
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AASN1058
ALYS1185
AGLU1344
BASN2058
BLYS2185
BGLU2344

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Increases basicity of active site His
ChainResidueDetails
AASP1295
BASP2295

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ec9
ChainResidueDetails
AHIS1325
AASP1348
AASP1295
ALYS1185
ALYS1187

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ec9
ChainResidueDetails
BLYS2185
BLYS2187
BASP2295
BHIS2325
BASP2348

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ec9
ChainResidueDetails
AGLU1344
ALYS1185
ALYS1187

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ec9
ChainResidueDetails
BLYS2185
BLYS2187
BGLU2344

site_idMCSA1
Number of Residues9
DetailsM-CSA 463
ChainResidueDetails
AASN1058electrostatic stabiliser
ALYS1185electrostatic stabiliser
ALYS1187proton acceptor, proton donor
AASP1216metal ligand
AGLU1242metal ligand
AGLU1268metal ligand
AASP1295electrostatic stabiliser, increase basicity, modifies pKa
AHIS1325proton acceptor, proton donor
AGLU1344electrostatic stabiliser

site_idMCSA2
Number of Residues9
DetailsM-CSA 463
ChainResidueDetails
BASN2058electrostatic stabiliser
BLYS2185electrostatic stabiliser
BLYS2187proton acceptor, proton donor
BASP2216metal ligand
BGLU2242metal ligand
BGLU2268metal ligand
BASP2295electrostatic stabiliser, increase basicity, modifies pKa
BHIS2325proton acceptor, proton donor
BGLU2344electrostatic stabiliser

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon