1TER
SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005516 | molecular_function | calmodulin binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0015459 | molecular_function | potassium channel regulator activity |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0044231 | cellular_component | host cell presynaptic membrane |
| A | 0090729 | molecular_function | toxin activity |
| A | 0099106 | molecular_function | ion channel regulator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NH2 A 22 |
| Chain | Residue |
| A | ILE8 |
| A | LYS21 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Peptide: {"description":"Tertiapin","featureId":"PRO_0000044539","evidences":[{"source":"PubMed","id":"9748337","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1980","firstPage":"359","lastPage":"365","volume":"6","journal":"Bioorg. Khim.","title":"Structure and presynaptic activity of tertiapin-neurotoxin from bee venom Apis mellifera.","authors":["Ovchinnikov Y.A.","Miroshnikov A.I.","Kudelin A.B.","Kostina M.B.","Boikov V.A.","Magazanik L.G.","Gotgilf I.M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Site: {"description":"Is responsible of pH dependence of the channel block"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Susceptible to oxidation","evidences":[{"source":"PubMed","id":"10572003","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
