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1QMD

calcium bound closed form alpha-toxin from Clostridium perfringens

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0044179biological_processhemolysis in another organism
A0046872molecular_functionmetal ion binding
A0090729molecular_functiontoxin 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
B0044179biological_processhemolysis in another organism
B0046872molecular_functionmetal ion binding
B0090729molecular_functiontoxin activity
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 Residues34
DetailsBINDING:
ChainResidueDetails
ATRP1
AHIS11
AHIS126
AASP130
AASP269
AGLY271
ATHR272
AASP273
AASP293
AASN294
AGLY296
AASN297
AASP298
AASP336
AALA337
BTRP1
BHIS11
BASP56
BHIS68
BHIS126
BASP130
BASP269
BGLY271
BTHR272
BASP273
BASP293
BASN294
BGLY296
BASN297
BASP298
BASP336
BALA337
AASP56
AHIS68

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AHIS136
AHIS148
AGLU152
BHIS136
BHIS148
BGLU152

221051

PDB entries from 2024-06-12

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