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5X9G

Crystal structure of the cytosolic domain of the Mg2+ channel MgtE in complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0015095molecular_functionmagnesium ion transmembrane transporter activity
A0015693biological_processmagnesium ion transport
A0016020cellular_componentmembrane
B0015095molecular_functionmagnesium ion transmembrane transporter activity
B0015693biological_processmagnesium ion transport
B0016020cellular_componentmembrane
C0015095molecular_functionmagnesium ion transmembrane transporter activity
C0015693biological_processmagnesium ion transport
C0016020cellular_componentmembrane
D0015095molecular_functionmagnesium ion transmembrane transporter activity
D0015693biological_processmagnesium ion transport
D0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ATP A 301
ChainResidue
ATYR170
APRO231
DGLU166
DTYR169
AVAL183
ASER185
AARG187
AASP188
AASN203
ALYS205
AVAL207
APHE227

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 302
ChainResidue
AASP91
AGLU166
ATHR244
AASP247

site_idAC3
Number of Residues2
Detailsbinding site for residue MG A 303
ChainResidue
AASP95
AGLY136

site_idAC4
Number of Residues13
Detailsbinding site for residue ATP B 301
ChainResidue
BTYR170
BVAL183
BSER185
BARG187
BASP188
BASN203
BLYS205
BVAL206
BVAL207
BPHE227
BPRO231
CGLU166
CTYR169

site_idAC5
Number of Residues2
Detailsbinding site for residue MG B 302
ChainResidue
BASP95
BGLY136

site_idAC6
Number of Residues3
Detailsbinding site for residue MG B 303
ChainResidue
BASP91
BGLU166
BASP247

site_idAC7
Number of Residues11
Detailsbinding site for residue ATP C 301
ChainResidue
BGLU166
BTYR169
CTYR170
CVAL183
CSER185
CARG187
CASP188
CASN203
CVAL207
CPHE227
CPRO231

site_idAC8
Number of Residues4
Detailsbinding site for residue MG C 302
ChainResidue
CASP91
CGLU166
CTHR244
CASP247

site_idAC9
Number of Residues2
Detailsbinding site for residue MG C 303
ChainResidue
CASP95
CGLY136

site_idAD1
Number of Residues11
Detailsbinding site for residue ATP D 301
ChainResidue
AGLU166
DTYR170
DVAL183
DSER185
DARG187
DASP188
DASN203
DVAL206
DVAL207
DPHE227
DPRO231

site_idAD2
Number of Residues4
Detailsbinding site for residue MG D 302
ChainResidue
DASP91
DGLU166
DTHR244
DASP247

site_idAD3
Number of Residues2
Detailsbinding site for residue MG D 303
ChainResidue
DASP95
DGLY136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715
ChainResidueDetails
AGLU59
CGLU216
CGLU255
CGLU258
DGLU59
DGLU216
DGLU255
DGLU258
AGLU216
AGLU255
AGLU258
BGLU59
BGLU216
BGLU255
BGLU258
CGLU59

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
ChainResidueDetails
AASP91
CASP95
CGLY136
CASP247
DASP91
DASP95
DGLY136
DASP247
AASP95
AGLY136
AASP247
BASP91
BASP95
BGLY136
BASP247
CASP91

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
ChainResidueDetails
ATYR170
BVAL207
CTYR170
CSER185
CARG187
CASP188
CVAL207
DTYR170
DSER185
DARG187
DASP188
ASER185
DVAL207
AARG187
AASP188
AVAL207
BTYR170
BSER185
BARG187
BASP188

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H
ChainResidueDetails
AALA223
DALA223
DASP226
DASP250
AASP226
AASP250
BALA223
BASP226
BASP250
CALA223
CASP226
CASP250

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9
ChainResidueDetails
AASP259
BASP259
CASP259
DASP259

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N
ChainResidueDetails
AGLU275
BGLU275
CGLU275
DGLU275

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PDB entries from 2024-07-10

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