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4YV5

Crystal Structure of Myotoxin II from Bothrops moojeni complexed to Suramin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0031640biological_processkilling of cells of another organism
A0035821biological_processmodulation of process of another organism
A0042130biological_processnegative regulation of T cell proliferation
A0042742biological_processdefense response to bacterium
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
A0050832biological_processdefense response to fungus
A0090729molecular_functiontoxin activity
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0031640biological_processkilling of cells of another organism
B0035821biological_processmodulation of process of another organism
B0042130biological_processnegative regulation of T cell proliferation
B0042742biological_processdefense response to bacterium
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonic acid secretion
B0050832biological_processdefense response to fungus
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 B 201
ChainResidue
BLYS20
BLYS115
BARG118
BSO4202

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 B 202
ChainResidue
BHOH351
BLYS16
BASN17
BLYS20
BSO4201
BHOH301

site_idAC3
Number of Residues12
Detailsbinding site for residue PE4 B 203
ChainResidue
ALYS7
ALEU10
AGLN11
AGLY15
ATYR75
ATRP77
BLYS7
BLEU10
BGLN11
BGLY15
BTYR75
BTRP77

site_idAC4
Number of Residues8
Detailsbinding site for residue 1PE B 204
ChainResidue
ATYR121
ALYS123
APRO125
BLEU2
BILE9
BCYS29
BGLY30
BHIS48

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 B 205
ChainResidue
BGLY33
BARG34
BLYS53
BHOH302

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 B 206
ChainResidue
ALYS38
ALYS116
ATYR117
BLYS116
BTYR117

site_idAC7
Number of Residues30
Detailsbinding site for residue SVR B 207
ChainResidue
APHE3
ALYS7
ALEU10
AASN17
APRO18
ACYS27
ALYS38
AARG72
APHE126
ACYS127
ALYS128
ASO4202
ASVR205
AHOH380
BASN114
BLYS115
BLYS116
BTYR119
BTYR121
BLEU122
BPHE126
BHOH305
BHOH311
BHOH316
BHOH320
BHOH338
BHOH347
BHOH352
BHOH356
BHOH361

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 A 201
ChainResidue
ALYS16
ALYS20
ALYS115
AARG118

site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 A 202
ChainResidue
ALYS16
AASN17
ALYS20
AHOH301
BSVR207

site_idAD1
Number of Residues8
Detailsbinding site for residue 1PE A 203
ChainResidue
AILE9
APRO18
ATYR22
AASN28
AGLY30
ACYS45
AHIS48
ALYS49

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 A 204
ChainResidue
AARG34
ALYS53
AHOH372

site_idAD3
Number of Residues33
Detailsbinding site for residue SVR A 205
ChainResidue
AHOH348
AHOH353
AHOH355
AHOH357
AHOH363
AHOH368
AHOH369
BPHE3
BGLY6
BLYS7
BLEU10
BASN17
BPRO18
BCYS27
BLYS36
BLYS38
BARG72
BPHE126
BCYS127
BLYS128
BSVR207
BHOH323
BHOH351
AASN114
ALYS115
ALYS116
ATYR119
ATYR121
ALEU122
APHE126
AHOH305
AHOH316
AHOH321

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCYvHKcC
ChainResidueDetails
BCYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAVaIC
ChainResidueDetails
BLEU95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000305|PubMed:29287778
ChainResidueDetails
BLYS16
BLYS20
ALYS16
ALYS20

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6, ECO:0000305|PubMed:29287778
ChainResidueDetails
BLYS115
BARG118
ALYS115
AARG118

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6
ChainResidueDetails
BLEU122
BPHE126
ALEU122
APHE126

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6
ChainResidueDetails
BLYS123
BLYS129
ALYS123
ALYS129

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PDB entries from 2024-08-07

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