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5ZX5

3.3 angstrom structure of mouse TRPM7 with EDTA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0051262biological_processprotein tetramerization
A0055085biological_processtransmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0051262biological_processprotein tetramerization
B0055085biological_processtransmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0051262biological_processprotein tetramerization
C0055085biological_processtransmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0051262biological_processprotein tetramerization
D0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue Y01 A 1301
ChainResidue
ASER1013
APHE1014
ATYR1080
BTYR923
BLEU977
BVAL990
BMET991
BGLY994

site_idAC2
Number of Residues9
Detailsbinding site for residue Y01 A 1302
ChainResidue
ALEU977
AVAL990
AMET991
AGLY994
AVAL1110
AGLN1114
DSER1013
DPHE1014
ATYR923

site_idAC3
Number of Residues8
Detailsbinding site for residue Y01 A 1303
ChainResidue
ALEU1012
ATRP1030
AALA1033
BMET868
BTHR871
BPHE872
BTYR973
BY011302

site_idAC4
Number of Residues9
Detailsbinding site for residue Y01 A 1304
ChainResidue
ALEU864
AMET868
ATHR871
APHE872
ATYR973
AY011305
DSER1029
DTRP1030
DALA1033

site_idAC5
Number of Residues9
Detailsbinding site for residue Y01 A 1305
ChainResidue
APHE856
ATRP857
APHE979
ALEU980
AVAL982
AASN983
AY011304
DLEU1009
DLEU1012

site_idAC6
Number of Residues8
Detailsbinding site for residue Y01 B 1301
ChainResidue
BSER1013
BLEU1076
BTYR1080
CPHE924
CLEU977
CVAL990
CMET991
CLYS995

site_idAC7
Number of Residues8
Detailsbinding site for residue Y01 B 1302
ChainResidue
AVAL1005
ALEU1012
AY011303
BTRP857
BLEU864
BLEU980
BVAL982
BASN983

site_idAC8
Number of Residues8
Detailsbinding site for residue Y01 C 1301
ChainResidue
BSER1029
BTRP1030
BALA1033
CMET868
CTHR871
CPHE872
CTYR973
CY011302

site_idAC9
Number of Residues6
Detailsbinding site for residue Y01 C 1302
ChainResidue
BALA1008
BLEU1012
CPHE856
CPHE979
CVAL982
CY011301

site_idAD1
Number of Residues6
Detailsbinding site for residue Y01 D 1301
ChainResidue
CSER1013
CVAL1079
DTYR923
DVAL990
DMET991
DGLY994

site_idAD2
Number of Residues8
Detailsbinding site for residue Y01 D 1302
ChainResidue
CPRO1028
CSER1029
CTRP1030
CALA1033
DTHR871
DPHE872
DTYR973
DY011303

site_idAD3
Number of Residues8
Detailsbinding site for residue Y01 D 1303
ChainResidue
CLEU1012
DTRP747
DPHE856
DTRP857
DPHE979
DVAL982
DASN983
DY011302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"37156763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SI2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues80
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"37156763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SI2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues76
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"37156763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SI2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues92
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"37156763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SI2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues72
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues92
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"37156763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SI2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues160
DetailsIntramembrane: {"description":"Pore-forming","evidences":[{"source":"PubMed","id":"37156763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SI2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues112
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"37156763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SI2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q96QT4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q96QT4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22222377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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