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4GV5

X-ray structure of crotamine, a cell-penetrating peptide from the Brazilian snake Crotalus durissus terrificus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0015459molecular_functionpotassium channel regulator activity
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044564biological_processenvenomation resulting in occlusion of the pore of voltage-gated potassium channel in another organism
A0050832biological_processdefense response to fungus
A0090729molecular_functiontoxin activity
B0005576cellular_componentextracellular region
B0015459molecular_functionpotassium channel regulator activity
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0044564biological_processenvenomation resulting in occlusion of the pore of voltage-gated potassium channel in another organism
B0050832biological_processdefense response to fungus
B0090729molecular_functiontoxin activity
C0005576cellular_componentextracellular region
C0015459molecular_functionpotassium channel regulator activity
C0031640biological_processkilling of cells of another organism
C0042742biological_processdefense response to bacterium
C0044564biological_processenvenomation resulting in occlusion of the pore of voltage-gated potassium channel in another organism
C0050832biological_processdefense response to fungus
C0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN A 101
ChainResidue
AILE17
AHOH204
CTYR1
CTRP34

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 102
ChainResidue
APRO13
ALYS14
AGLU15
BPRO21
CPRO13

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 103
ChainResidue
ALYS14
ATRP32
AARG33
BPRO21
BSER22

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 104
ChainResidue
AGLN3
ATRP32
AARG33
AHOH215

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 101
ChainResidue
BLYS2
BGLN3
BTRP32
BARG33
BHOH209
BHOH211

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 102
ChainResidue
BTYR1
BHIS10
BCYS11
BHOH213
CARG31
CTRP32

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN B 103
ChainResidue
BPHE12
BPRO13
BILE17
BGLY42
CGOL103

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 101
ChainResidue
APHE12
APRO13
ALYS16
CHIS10
CCYS11
CHOH204

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SCN C 102
ChainResidue
CTRP32
CARG33

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 103
ChainResidue
BPHE12
BGLY42
BSCN103
CARG31
CTRP32
CARG33
CTRP34

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 104
ChainResidue
BLEU19
BPRO20
BPRO21
CPRO13
CLYS14
CGLU15
CLYS16

Functional Information from PROSITE/UniProt
site_idPS00459
Number of Residues38
DetailsMYOTOXINS_1 Myotoxins signature. KqCHkKggHCfpKekiClppssdfgKmdCrwRwKCCKK
ChainResidueDetails
ALYS2-LYS39

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsSITE: Involved in the interaction surface toward Kv => ECO:0000305
ChainResidueDetails
ASER23
CASP24
CARG33
CTRP34
AASP24
AARG33
ATRP34
BSER23
BASP24
BARG33
BTRP34
CSER23

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PDB entries from 2024-07-10

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