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6ZFZ

Structure of M1-StaR-T4L in complex with 77-LH-28-1 at 2.17A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
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 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 Residues33
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:32646996, ECO:0007744|PDB:6WJC
ChainResidueDetails
ASER49-TYR62
AASP122-ALA142

site_idSWS_FT_FI2
Number of Residues21
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:32646996, ECO:0007744|PDB:6WJC
ChainResidueDetails
APHE63-VAL84

site_idSWS_FT_FI3
Number of Residues36
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:32646996, ECO:0007744|PDB:6WJC
ChainResidueDetails
ATYR85-ALA95
AGLN165-GLN185
ACYS391-GLU397

site_idSWS_FT_FI4
Number of Residues25
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:32646996, ECO:0007744|PDB:6WJC
ChainResidueDetails
ALEU96-PHE121

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:32646996, ECO:0007744|PDB:6WJC
ChainResidueDetails
ALEU143-TRP164

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:32646996, ECO:0007744|PDB:6WJC
ChainResidueDetails
APRO186-TRP209

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:32646996, ECO:0007744|PDB:6WJC
ChainResidueDetails
ALEU367-PHE390

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:32646996, ECO:0007744|PDB:6WJC
ChainResidueDetails
ATHR398-LEU420

site_idSWS_FT_FI9
Number of Residues4
DetailsSITE: Subtype-specific residue that binds to snake venom muscarinic toxin 7 => ECO:0000269|PubMed:32646996
ChainResidueDetails
ALEU174
AGLU397
AGLU401
AGLU170

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Binds to snake venom muscarinic toxin 7 => ECO:0000269|PubMed:32646996
ChainResidueDetails
ATHR172

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000255
ChainResidueDetails
ATHR428

site_idSWS_FT_FI12
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI13
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1020

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI15
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

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

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PDB entries from 2024-05-29

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