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1QMD

calcium bound closed form alpha-toxin from Clostridium perfringens

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004629molecular_functionphospholipase C activity
A0005576cellular_componentextracellular region
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0031640biological_processkilling of cells of another organism
A0034480molecular_functionphosphatidylcholine phospholipase C activity
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0090729molecular_functiontoxin activity
A0140324
B0003824molecular_functioncatalytic activity
B0004629molecular_functionphospholipase C activity
B0005576cellular_componentextracellular region
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0031640biological_processkilling of cells of another organism
B0034480molecular_functionphosphatidylcholine phospholipase C activity
B0035821biological_processmodulation of process of another organism
B0046872molecular_functionmetal ion binding
B0090729molecular_functiontoxin activity
B0140324
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ATRP1
AHIS11
AASP130
AZN402
AHOH2023

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AZN401
AHOH2023
AASP56
AHIS68
AHIS126
AASP130

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP269
AGLY271
AASP336
AALA337
BGLU32

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
AASP293
AASN294
AGLY296
AASP298

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 405
ChainResidue
ATHR272
AASP273
AASN297
AASP298
AHOH2141

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BTRP1
BHIS11
BASP130
BZN402
BHOH2152

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BASP56
BHIS68
BHIS126
BASP130
BZN401
BHOH2152

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BASP293
BASN294
BGLY296
BASP298

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
AGLU32
AHOH2011
BASP269
BGLY271
BASP336
BALA337

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 405
ChainResidue
BTHR272
BASP273
BASN297
BASP298

Functional Information from PROSITE/UniProt
site_idPS00384
Number of Residues14
DetailsPROKAR_ZN_DEPEND_PLPC_1 Prokaryotic zinc-dependent phospholipase C signature. HYfGDIDtPyHPaN
ChainResidueDetails
AHIS126-ASN139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues498
DetailsDomain: {"description":"Zn-dependent PLC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00678","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues228
DetailsDomain: {"description":"PLAT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00152","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsRegion: {"description":"Linker"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues34
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ah7
ChainResidueDetails
AASP56

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ah7
ChainResidueDetails
BASP56

247536

PDB entries from 2026-01-14

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