Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ZXD

wild-type lysenin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0031640biological_processkilling of cells of another organism
A0035821biological_processmodulation of process of another organism
A0042742biological_processdefense response to bacterium
A0044218cellular_componentother organism cell membrane
A0090729molecular_functiontoxin activity
B0005576cellular_componentextracellular region
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0031640biological_processkilling of cells of another organism
B0035821biological_processmodulation of process of another organism
B0042742biological_processdefense response to bacterium
B0044218cellular_componentother organism cell membrane
B0090729molecular_functiontoxin activity
C0005576cellular_componentextracellular region
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0031640biological_processkilling of cells of another organism
C0035821biological_processmodulation of process of another organism
C0042742biological_processdefense response to bacterium
C0044218cellular_componentother organism cell membrane
C0090729molecular_functiontoxin activity
D0005576cellular_componentextracellular region
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0031640biological_processkilling of cells of another organism
D0035821biological_processmodulation of process of another organism
D0042742biological_processdefense response to bacterium
D0044218cellular_componentother organism cell membrane
D0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 398
ChainResidue
ATYR225
ASER227
AASP228

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 467
ChainResidue
AALA18
ASER151

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES A 921
ChainResidue
ALYS249
ASER250
APRO252
AASP257
ATHR63
ASER65
AASP68
AASN248

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 468
ChainResidue
BASN248

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES B 921
ChainResidue
BTHR63
BSER65
BASP68
BASN248
BLYS249
BSER250
BPRO252
BASP257

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 398
ChainResidue
CGLU22
CTYR24
CVAL25

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 546
ChainResidue
CLYS249
CASP257

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 467
ChainResidue
AGLY30
ASER31
DTYR24
DMG470

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES D 921
ChainResidue
DTHR66
DASP68
DLYS249
DSER250
DPRO252
DASP257

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 466
ChainResidue
AVAL14
ASER62

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 469
ChainResidue
ASER186
ATRP187

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 468
ChainResidue
AVAL19
ATRP20
AGLN147
AVAL148
AMG470
BTYR265

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 470
ChainResidue
ASO4468
BLYS264
BTYR265

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 500
ChainResidue
AGLN143

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AGLU13
AASP15

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 502
ChainResidue
AGLU174
ALYS290

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 465
ChainResidue
BVAL14
BASP15
BILE60
BSER62
BTHR63
BMG470

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 500
ChainResidue
BALA18
BVAL148
BSER151

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 470
ChainResidue
BSO4465

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 472
ChainResidue
BSER59
BTHR66

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 473
ChainResidue
BTYR225
BSER227
BASP228

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 547
ChainResidue
BGLU76
CGLU22

site_idCC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA D 500
ChainResidue
BLYS42
DGLU102

site_idCC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG D 470
ChainResidue
DVAL25
DSO4467

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. ETRTVTATHSI
ChainResidueDetails
AGLU50-ILE60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:22819216
ChainResidueDetails
ALYS185
CSER227
CTYR233
CTYR282
DLYS185
DSER227
DTYR233
DTYR282
ASER227
ATYR233
ATYR282
BLYS185
BSER227
BTYR233
BTYR282
CLYS185

site_idSWS_FT_FI2
Number of Residues12
DetailsSITE: Crucial for binding sphingomyelin and inducing hemolysis => ECO:0000269|PubMed:15274631
ChainResidueDetails
ATRP20
DTRP20
DTRP245
DTRP291
ATRP245
ATRP291
BTRP20
BTRP245
BTRP291
CTRP20
CTRP245
CTRP291

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Crucial for binding sphingomyelin and important for inducing hemolysis => ECO:0000269|PubMed:15274631
ChainResidueDetails
ATRP187
BTRP187
CTRP187
DTRP187

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Important for activity
ChainResidueDetails
APHE209
BPHE209
CPHE209
DPHE209

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon