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4NTO

Crystal structure of D60A mutant of Arabidopsis ACD11 (accelerated-cell-death 11) complexed with C2 ceramide-1-phosphate (d18:1/2:0) at 2.15 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006869biological_processlipid transport
A0008219biological_processcell death
A0008289molecular_functionlipid binding
A0009751biological_processresponse to salicylic acid
A0015914biological_processphospholipid transport
A0042742biological_processdefense response to bacterium
A0120009biological_processintermembrane lipid transfer
A0120013molecular_functionlipid transfer activity
A0140338molecular_functionsphingomyelin transfer activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006869biological_processlipid transport
B0008219biological_processcell death
B0008289molecular_functionlipid binding
B0009751biological_processresponse to salicylic acid
B0015914biological_processphospholipid transport
B0042742biological_processdefense response to bacterium
B0120009biological_processintermembrane lipid transfer
B0120013molecular_functionlipid transfer activity
B0140338molecular_functionsphingomyelin transfer activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0006869biological_processlipid transport
C0008219biological_processcell death
C0008289molecular_functionlipid binding
C0009751biological_processresponse to salicylic acid
C0015914biological_processphospholipid transport
C0042742biological_processdefense response to bacterium
C0120009biological_processintermembrane lipid transfer
C0120013molecular_functionlipid transfer activity
C0140338molecular_functionsphingomyelin transfer activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1PW A 301
ChainResidue
AMET59
CLEU153
CTYR156
ALYS64
AARG99
AARG103
AHIS143
AILE147
A1PW302
AHOH421
AHOH502

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PW A 302
ChainResidue
AILE147
A1PW301
CTRP145
CARG148
CTYR156

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 303
ChainResidue
APRO141
C1PW301

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1PW B 301
ChainResidue
ALEU153
ATYR156
BGLY144
BTRP145
BTRP145
BALA146
BILE147
BARG148
B1PW302
BHOH490
C1PW302

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 1PW B 302
ChainResidue
ATYR156
BMET59
BALA60
BLYS64
BARG99
BARG103
BILE147
B1PW301

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG B 303
ChainResidue
BSER152

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1PW C 301
ChainResidue
ATRP145
AARG148
APEG303
AHOH473
BTYR156
CHIS142
CHIS143
CGLY144
CILE147
CALA150
CHOH437
CHOH458

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1PW C 302
ChainResidue
BTYR156
B1PW301
CPHE56
CMET59
CALA60
CLYS64
CARG99
CARG103
CILE147
CHOH437
CHOH439

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:24412362
ChainResidueDetails
AALA60
BHIS143
CALA60
CLYS64
CARG99
CARG103
CHIS143
ALYS64
AARG99
AARG103
AHIS143
BALA60
BLYS64
BARG99
BARG103

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PDB entries from 2024-10-30

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