1SXM
SCORPION TOXIN (NOXIUSTOXIN) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL AND LOW AFFINITY FOR CALCIUM DEPENDENT POTASSIUM CHANNEL (NMR AT 20 DEGREES, PH3.5, 39 STRUCTURES)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0008200 | molecular_function | ion channel inhibitor activity |
| A | 0015459 | molecular_function | potassium channel regulator activity |
| A | 0035821 | biological_process | modulation of process of another organism |
| 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 | 1 |
| Details | BINDING SITE FOR RESIDUE NH2 A 40 |
| Chain | Residue |
| A | ASN39 |
Functional Information from PROSITE/UniProt
| site_id | PS01138 |
| Number of Residues | 24 |
| Details | SCORP_SHORT_TOXIN Scorpion short toxins signature. CskpCkelygssagAKCMngkCkC |
| Chain | Residue | Details |
| A | CYS13-CYS36 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 38 |
| Details | Peptide: {"description":"Potassium channel toxin alpha-KTx 2.1","featureId":"PRO_0000044905","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1982","firstPage":"285","lastPage":"289","volume":"47","journal":"Carlsberg Res. Commun.","title":"The primary structure of noxiustoxin. A K channel blocking peptide, purified from the venom of the scorpion Centruroides noxius Hoffmann.","authors":["Possani L.D.","Martin B.M.","Svendsen I."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Region: {"description":"Interaction with Ca(2+)-activated K(+) channels","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Basic residue of the functional dyad","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Aromatic residue of the functional dyad","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Asparagine amide","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1993","firstPage":"101","lastPage":"102","publisher":"Escom Science Publishers","address":"Leiden","bookName":"Peptides 1992","title":"Structure revision of the scorpion toxin noxiustoxin through total chemical synthesis.","editors":["Schneider C.H.","Eberles A.N."],"authors":["Nutt R.F.","Arison B.H.","Smith J.S."]}}]} |
| Chain | Residue | Details |
