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6ZG4

Structure of M1-StaR-T4L in complex with HTL0009936 at 2.35A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue QK8 A 1201
ChainResidue
ALEU81
ACYS178
ATRP378
ATYR404
ATYR408
AHOH1327
AHOH1347
ATYR82
ATYR85
AALA101
ALEU102
AASP105
ATYR106
ASER109
AASN110

site_idAC2
Number of Residues8
Detailsbinding site for residue OLA A 1202
ChainResidue
ALEU104
AVAL107
ALEU143
AGLY147
ATRP150
APHE154
ACYS394
AOLA1203

site_idAC3
Number of Residues2
Detailsbinding site for residue OLA A 1203
ChainResidue
ATRP150
AOLA1202

site_idAC4
Number of Residues3
Detailsbinding site for residue OLA A 1204
ChainResidue
AGLU401
ATRP405
AOLA1211

site_idAC5
Number of Residues4
Detailsbinding site for residue OLA A 1205
ChainResidue
AMET114
ALEU118
AARG141
AMET145

site_idAC6
Number of Residues4
Detailsbinding site for residue OLA A 1206
ChainResidue
AALA76
APHE77
ALEU81
ALEU93

site_idAC7
Number of Residues6
Detailsbinding site for residue OLA A 1207
ChainResidue
AGLU1011
AILE1029
AGLY1030
AVAL1103
APHE1104
AGLN1105

site_idAC8
Number of Residues2
Detailsbinding site for residue PGE A 1208
ChainResidue
ATYR85
AGLU401

site_idAC9
Number of Residues5
Detailsbinding site for residue PO4 A 1209
ChainResidue
APHE1114
ATHR1115
AASN1116
ASER1117
AASN1132

site_idAD1
Number of Residues4
Detailsbinding site for residue PO4 A 1210
ChainResidue
ATHR1142
APRO1143
AASN1144
AARG1145

site_idAD2
Number of Residues1
Detailsbinding site for residue OLA A 1211
ChainResidue
AOLA1204

site_idAD3
Number of Residues1
Detailsbinding site for residue OLA A 1212
ChainResidue
AGLU24

site_idAD4
Number of Residues8
Detailsbinding site for residue OLA A 1213
ChainResidue
ALEU93
AALA95
ALEU96
AALA175
ACYS205
ATYR208
ATRP209
ATYR212

site_idAD5
Number of Residues5
Detailsbinding site for residue OLA A 1214
ChainResidue
AALA38
ATYR166
ALEU167
ALEU420
AHOH1332

site_idAD6
Number of Residues4
Detailsbinding site for residue OLA A 1215
ChainResidue
ALEU156
APHE163
AILE413
ALEU420

site_idAD7
Number of Residues5
Detailsbinding site for residue PO4 A 1216
ChainResidue
AARG123
AARG134
ALYS1065
AHOH1326
AHOH1351

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. AAVmNLLLISFDRYFsV
ChainResidueDetails
AALA111-VAL127

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues33
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues36
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues41
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues9
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues15
DetailsCompositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsSite: {"description":"Subtype-specific residue that binds to snake venom muscarinic toxin 7","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsSite: {"description":"Binds to snake venom muscarinic toxin 7","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P12657","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

239803

PDB entries from 2025-08-06

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