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5X9H

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005886cellular_componentplasma membrane
A0006812biological_processmonoatomic cation transport
A0008324molecular_functionmonoatomic cation transmembrane transporter activity
A0015095molecular_functionmagnesium ion transmembrane transporter activity
A0015693biological_processmagnesium ion transport
A0016020cellular_componentmembrane
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0098655biological_processmonoatomic cation transmembrane transport
A1903830biological_processmagnesium ion transmembrane transport
B0000287molecular_functionmagnesium ion binding
B0005886cellular_componentplasma membrane
B0006812biological_processmonoatomic cation transport
B0008324molecular_functionmonoatomic cation transmembrane transporter activity
B0015095molecular_functionmagnesium ion transmembrane transporter activity
B0015693biological_processmagnesium ion transport
B0016020cellular_componentmembrane
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0098655biological_processmonoatomic cation transmembrane transport
B1903830biological_processmagnesium ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ATP A 501
ChainResidue
ATYR170
APRO231
BGLU166
BTYR169
AVAL183
ASER185
AARG187
AASN203
ALYS205
AVAL206
AVAL207
APHE227

site_idAC2
Number of Residues1
Detailsbinding site for residue MG A 502
ChainResidue
AASP432

site_idAC3
Number of Residues1
Detailsbinding site for residue MG A 504
ChainResidue
AASP259

site_idAC4
Number of Residues2
Detailsbinding site for residue MG A 505
ChainResidue
AASP91
AASP247

site_idAC5
Number of Residues3
Detailsbinding site for residue MG A 506
ChainResidue
AALA223
AASP226
BASP250

site_idAC6
Number of Residues2
Detailsbinding site for residue MG A 507
ChainResidue
AASP95
AGLY136

site_idAC7
Number of Residues2
Detailsbinding site for residue MG A 508
ChainResidue
AGLU59
BASP226

site_idAC8
Number of Residues2
Detailsbinding site for residue MG A 509
ChainResidue
AASP226
BGLU59

site_idAC9
Number of Residues12
Detailsbinding site for residue ATP B 501
ChainResidue
AGLU166
ATYR169
BTYR170
BVAL183
BSER185
BARG187
BASP188
BASN203
BLYS205
BVAL206
BVAL207
BPHE227

site_idAD1
Number of Residues3
Detailsbinding site for residue MG B 502
ChainResidue
BALA223
BASP224
BASP226

site_idAD2
Number of Residues3
Detailsbinding site for residue MG B 504
ChainResidue
BGLU216
BASP259
BASP418

site_idAD3
Number of Residues3
Detailsbinding site for residue MG B 505
ChainResidue
BASP91
BGLU166
BASP247

site_idAD4
Number of Residues2
Detailsbinding site for residue MG B 506
ChainResidue
BASP95
BGLY136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues610
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295
ChainResidueDetails
AMET1-LEU283
AILE338-ASP351
APHE410-ALA420
BMET1-LEU283
BILE338-ASP351
BPHE410-ALA420

site_idSWS_FT_FI2
Number of Residues234
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB
ChainResidueDetails
AALA284-PHE306
BLEU421-ALA443
ALEU316-LEU337
ATRP352-ASP381
ALEU386-PRO409
ALEU421-ALA443
BALA284-PHE306
BLEU316-LEU337
BTRP352-ASP381
BLEU386-PRO409

site_idSWS_FT_FI3
Number of Residues34
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295
ChainResidueDetails
AGLU307-ALA315
AGLY382-LEU385
AARG444-VAL450
BGLU307-ALA315
BGLY382-LEU385
BARG444-VAL450

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715
ChainResidueDetails
AGLU59
BASP432
AGLU216
AGLU255
AGLU258
AASP432
BGLU59
BGLU216
BGLU255
BGLU258

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
ChainResidueDetails
AASP91
AASP95
AGLY136
AASP247
BASP91
BASP95
BGLY136
BASP247

site_idSWS_FT_FI6
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
ChainResidueDetails
ATYR170
BVAL207
ASER185
AARG187
AASP188
AVAL207
BTYR170
BSER185
BARG187
BASP188

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H
ChainResidueDetails
AALA223
AASP226
AASP250
BALA223
BASP226
BASP250

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9
ChainResidueDetails
AASP259
AASP418
BASP259
BASP418

site_idSWS_FT_FI9
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N
ChainResidueDetails
AGLU275
BHIS383
AGLN304
AGLU307
AGLU311
AHIS383
BGLU275
BGLN304
BGLU307
BGLU311

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19798051
ChainResidueDetails
AALA428
BALA428

218853

数据于2024-04-24公开中

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