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

5N78

Crystal structure of the cytosolic domain of the CorA Mg2+ channel from Escherichia coli in complex with magnesium and cobalt hexammine

Functional Information from GO Data
ChainGOidnamespacecontents
A0006824biological_processcobalt ion transport
A0015087molecular_functioncobalt ion transmembrane transporter activity
A0015095molecular_functionmagnesium ion transmembrane transporter activity
A0015693biological_processmagnesium ion transport
A0016020cellular_componentmembrane
A0030001biological_processmetal ion transport
A0046873molecular_functionmetal ion transmembrane transporter activity
A0055085biological_processtransmembrane transport
B0006824biological_processcobalt ion transport
B0015087molecular_functioncobalt ion transmembrane transporter activity
B0015095molecular_functionmagnesium ion transmembrane transporter activity
B0015693biological_processmagnesium ion transport
B0016020cellular_componentmembrane
B0030001biological_processmetal ion transport
B0046873molecular_functionmetal ion transmembrane transporter activity
B0055085biological_processtransmembrane transport
C0006824biological_processcobalt ion transport
C0015087molecular_functioncobalt ion transmembrane transporter activity
C0015095molecular_functionmagnesium ion transmembrane transporter activity
C0015693biological_processmagnesium ion transport
C0016020cellular_componentmembrane
C0030001biological_processmetal ion transport
C0046873molecular_functionmetal ion transmembrane transporter activity
C0055085biological_processtransmembrane transport
D0006824biological_processcobalt ion transport
D0015087molecular_functioncobalt ion transmembrane transporter activity
D0015095molecular_functionmagnesium ion transmembrane transporter activity
D0015693biological_processmagnesium ion transport
D0016020cellular_componentmembrane
D0030001biological_processmetal ion transport
D0046873molecular_functionmetal ion transmembrane transporter activity
D0055085biological_processtransmembrane transport
E0006824biological_processcobalt ion transport
E0015087molecular_functioncobalt ion transmembrane transporter activity
E0015095molecular_functionmagnesium ion transmembrane transporter activity
E0015693biological_processmagnesium ion transport
E0016020cellular_componentmembrane
E0030001biological_processmetal ion transport
E0046873molecular_functionmetal ion transmembrane transporter activity
E0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue MG A 301
ChainResidue
AASP58
AHOH403

site_idAC2
Number of Residues5
Detailsbinding site for residue NCO A 303
ChainResidue
AASP146
AGLU149
AASN150
CGLU57
EGLN21

site_idAC3
Number of Residues5
Detailsbinding site for residue NCO A 304
ChainResidue
AASN150
AILE184
EGLU19
AGLU81
AGLU147

site_idAC4
Number of Residues2
Detailsbinding site for residue NCO A 305
ChainResidue
ALEU50
AGLU55

site_idAC5
Number of Residues4
Detailsbinding site for residue MG B 301
ChainResidue
BASP58
BHOH402
EASP146
EHOH402

site_idAC6
Number of Residues5
Detailsbinding site for residue PG0 B 302
ChainResidue
BARG189
BMET193
BHOH409
EPRO228
EHIS229

site_idAC7
Number of Residues11
Detailsbinding site for residue NCO B 303
ChainResidue
AASN249
AGLN252
BASN249
BGLN252
BHOH403
CASN249
CGLN252
DASN249
DGLN252
EASN249
EGLN252

site_idAC8
Number of Residues3
Detailsbinding site for residue NCO B 304
ChainResidue
BSER49
BGLU55
BASP70

site_idAC9
Number of Residues3
Detailsbinding site for residue NCO B 305
ChainResidue
AGLU57
BGLU149
BASN150

site_idAD1
Number of Residues4
Detailsbinding site for residue MG C 301
ChainResidue
AASP146
CASP58
CHOH401
CHOH407

site_idAD2
Number of Residues5
Detailsbinding site for residue PG0 C 302
ChainResidue
APRO228
ASER232
CARG189
CMET193
CHOH408

site_idAD3
Number of Residues3
Detailsbinding site for residue NCO C 303
ChainResidue
CLEU50
CGLU55
CASP70

site_idAD4
Number of Residues2
Detailsbinding site for residue NCO C 304
ChainResidue
CGLU81
CASP85

site_idAD5
Number of Residues3
Detailsbinding site for residue MG D 301
ChainResidue
DASP58
DHOH403
DHOH412

site_idAD6
Number of Residues4
Detailsbinding site for residue NCO D 302
ChainResidue
DGLU81
DASP85
DGLU147
DASN150

site_idAD7
Number of Residues3
Detailsbinding site for residue NCO D 303
ChainResidue
DASP146
DGLU149
EGLU57

site_idAD8
Number of Residues3
Detailsbinding site for residue NCO D 304
ChainResidue
DLEU50
DGLU55
DASP70

site_idAD9
Number of Residues4
Detailsbinding site for residue MG E 301
ChainResidue
DHOH402
EASP58
EGLU60
EHOH404

site_idAE1
Number of Residues6
Detailsbinding site for residue PG0 E 302
ChainResidue
DPRO228
DHIS229
DSER232
EARG189
EMET193
EARG197

site_idAE2
Number of Residues3
Detailsbinding site for residue NCO E 303
ChainResidue
EGLU81
EGLU147
EASN150

site_idAE3
Number of Residues3
Detailsbinding site for residue NCO E 304
ChainResidue
EASP146
EGLU149
EASN150

site_idAE4
Number of Residues1
Detailsbinding site for residue NCO E 305
ChainResidue
EGLU55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1265
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-ARG254
BMET1-ARG254
CMET1-ARG254
DMET1-ARG254
EMET1-ARG254

site_idSWS_FT_FI2
Number of Residues5
DetailsSITE: Essential for ion permeation => ECO:0000250|UniProtKB:Q9WZ31
ChainResidueDetails
AASN253
BASN253
CASN253
DASN253
EASN253

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon