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6EBX

STRUCTURE DETERMINATION OF A DIMERIC FORM OF ERABUTOXIN B, CRYSTALLIZED FROM THIOCYANATE SOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0030550molecular_functionacetylcholine receptor inhibitor activity
A0035821biological_processmodulation of process of another organism
A0090729molecular_functiontoxin activity
A0099106molecular_functionion channel regulator activity
B0005576cellular_componentextracellular region
B0030550molecular_functionacetylcholine receptor inhibitor activity
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
B0099106molecular_functionion channel regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SCN B 63
ChainResidue
AARG33
BSER23
BCYS54

site_idCMA
Number of Residues13
Details
ChainResidue
ACYS3
APHE4
ACYS17
ACYS24
ATYR25
AGLY40
ACYS41
AGLY42
ACYS43
ACYS54
ACYS55
ACYS60
AASN61

site_idCMB
Number of Residues13
Details
ChainResidue
BCYS3
BPHE4
BCYS17
BCYS24
BTYR25
BGLY40
BCYS41
BGLY42
BCYS43
BCYS54
BCYS55
BCYS60
BASN61

site_idFNA
Number of Residues4
Details
ChainResidue
ALYS27
ATRP29
AARG33
ALYS47

site_idFNB
Number of Residues4
Details
ChainResidue
BLYS27
BTRP29
BARG33
BLYS47

site_idRCA
Number of Residues20
Details
ChainResidue
ATYR25
AGLY40
ACYS41
AGLY42
ACYS43
APRO44
AVAL46
ALYS47
AGLY49
AILE50
ALEU52
ALYS27
ACYS54
ATRP29
AASP31
APHE32
AARG33
AGLY34
AILE36
AGLU38

site_idRCB
Number of Residues20
Details
ChainResidue
BTYR25
BLYS27
BTRP29
BASP31
BPHE32
BARG33
BGLY34
BILE36
BGLU38
BGLY40
BCYS41
BGLY42
BCYS43
BPRO44
BVAL46
BLYS47
BGLY49
BILE50
BLEU52
BCYS54

Functional Information from PROSITE/UniProt
site_idPS00272
Number of Residues19
DetailsSNAKE_TOXIN Snake toxins signature. GCg..CPtvkpgikls.CCesE
ChainResidueDetails
AGLY40-GLU58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsRegion: {"description":"Loop I","evidences":[{"source":"UniProtKB","id":"P60775","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsRegion: {"description":"Stretch between loop I and loop II","evidences":[{"source":"UniProtKB","id":"P60775","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues34
DetailsRegion: {"description":"Loop II","evidences":[{"source":"UniProtKB","id":"P60775","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues22
DetailsRegion: {"description":"Loop III","evidences":[{"source":"UniProtKB","id":"P60775","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsSite: {"description":"Moderately important residue for binding to acetylcholine receptor","evidences":[{"source":"UniProtKB","id":"P60775","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsSite: {"description":"Very important residue for binding to acetylcholine receptor","evidences":[{"source":"UniProtKB","id":"P60775","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsSite: {"description":"Key residue for binding to acetylcholine receptor","evidences":[{"source":"UniProtKB","id":"P60775","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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