4NTG
Crystal structure of D60A mutant of Arabidopsis ACD11 (accelerated-cell-death 11) complexed with C12 ceramide-1-phosphate (d18:1/12:0) at 2.55 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006869 | biological_process | lipid transport |
| A | 0008219 | biological_process | cell death |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009751 | biological_process | response to salicylic acid |
| A | 0015914 | biological_process | phospholipid transport |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0120009 | biological_process | intermembrane lipid transfer |
| A | 0120013 | molecular_function | lipid transfer activity |
| A | 0140338 | molecular_function | sphingomyelin transfer activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006869 | biological_process | lipid transport |
| B | 0008219 | biological_process | cell death |
| B | 0008289 | molecular_function | lipid binding |
| B | 0009751 | biological_process | response to salicylic acid |
| B | 0015914 | biological_process | phospholipid transport |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0120009 | biological_process | intermembrane lipid transfer |
| B | 0120013 | molecular_function | lipid transfer activity |
| B | 0140338 | molecular_function | sphingomyelin transfer activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 1PZ A 301 |
| Chain | Residue |
| A | ALA53 |
| A | PHE139 |
| A | HIS143 |
| A | ILE147 |
| A | ALA150 |
| A | VAL151 |
| A | LEU153 |
| A | HOH401 |
| A | HOH403 |
| A | HOH406 |
| A | HOH409 |
| A | PHE54 |
| A | HOH412 |
| B | GLY144 |
| A | ALA57 |
| A | ALA60 |
| A | TYR61 |
| A | LYS64 |
| A | ARG99 |
| A | ARG103 |
| A | MET110 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 1PZ B 301 |
| Chain | Residue |
| A | GLY144 |
| B | ALA53 |
| B | ALA57 |
| B | LYS64 |
| B | ARG99 |
| B | ARG103 |
| B | MET110 |
| B | PHE139 |
| B | HIS143 |
| B | ILE147 |
| B | ALA150 |
| B | LEU153 |
| B | HOH404 |
| B | HOH412 |
| B | HOH421 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24412362 |
| Chain | Residue | Details |
| A | ALA60 | |
| B | HIS143 | |
| A | LYS64 | |
| A | ARG99 | |
| A | ARG103 | |
| A | HIS143 | |
| B | ALA60 | |
| B | LYS64 | |
| B | ARG99 | |
| B | ARG103 |
