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1R1G

Crystal Structure of the Scorpion Toxin BmBKTtx1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008200molecular_functionion channel inhibitor activity
A0015459molecular_functionpotassium channel regulator activity
A0035821biological_processmodulation of process of another organism
A0090729molecular_functiontoxin activity
B0005576cellular_componentextracellular region
B0008200molecular_functionion channel inhibitor activity
B0015459molecular_functionpotassium channel regulator activity
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
Functional Information from PROSITE/UniProt
site_idPS01138
Number of Residues22
DetailsSCORP_SHORT_TOXIN Scorpion short toxins signature. CrvkCvamgfss..GKCInskCkC
ChainResidueDetails
ACYS8-CYS29

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Crucial for toxin binding => ECO:0000305
ChainResidueDetails
AARG9
AMLY11
BARG9
BMLY11

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Basic residue of the functional dyad => ECO:0000250
ChainResidueDetails
AMLY21
BMLY21

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Aromatic residue of the functional dyad => ECO:0000250
ChainResidueDetails
ATYR30
BTYR30

224931

PDB entries from 2024-09-11

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