4NTI
Crystal structure of D60N mutant of Arabidopsis ACD11 (accelerated-cell-death 11) complexed with C12 ceramide-1-phosphate (d18:1/12:0) at 2.9 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009751 | biological_process | response to salicylic acid |
| A | 0015914 | biological_process | phospholipid transport |
| A | 0035627 | biological_process | ceramide transport |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0120009 | biological_process | intermembrane lipid transfer |
| A | 0120013 | molecular_function | lipid transfer activity |
| A | 0120014 | molecular_function | phospholipid transfer activity |
| A | 0120016 | molecular_function | sphingolipid transfer activity |
| A | 0140338 | molecular_function | sphingomyelin transfer activity |
| A | 1902387 | molecular_function | ceramide 1-phosphate binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009751 | biological_process | response to salicylic acid |
| B | 0015914 | biological_process | phospholipid transport |
| B | 0035627 | biological_process | ceramide transport |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0120009 | biological_process | intermembrane lipid transfer |
| B | 0120013 | molecular_function | lipid transfer activity |
| B | 0120014 | molecular_function | phospholipid transfer activity |
| B | 0120016 | molecular_function | sphingolipid transfer activity |
| B | 0140338 | molecular_function | sphingomyelin transfer activity |
| B | 1902387 | molecular_function | ceramide 1-phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 1PZ A 301 |
| Chain | Residue |
| A | LEU46 |
| A | ARG103 |
| A | MET110 |
| A | VAL111 |
| A | LEU114 |
| A | ALA131 |
| A | TYR135 |
| A | PHE139 |
| A | HIS143 |
| A | HOH409 |
| A | PHE47 |
| A | LEU50 |
| A | PHE54 |
| A | PHE56 |
| A | ASN60 |
| A | TYR61 |
| A | LYS64 |
| A | ARG99 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PZ A 302 |
| Chain | Residue |
| A | TRP145 |
| A | 1PZ303 |
| B | ALA146 |
| B | ILE147 |
| B | 1PZ301 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PZ A 303 |
| Chain | Residue |
| A | LYS149 |
| A | 1PZ302 |
| B | MET59 |
| B | PEG304 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1PZ B 301 |
| Chain | Residue |
| A | 1PZ302 |
| B | ALA53 |
| B | ALA57 |
| B | ASN60 |
| B | LYS64 |
| B | ARG99 |
| B | ARG103 |
| B | PHE139 |
| B | HIS143 |
| B | ALA150 |
| B | LEU153 |
| B | HOH403 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 304 |
| Chain | Residue |
| A | TYR156 |
| A | 1PZ303 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 305 |
| Chain | Residue |
| A | GLY48 |
| B | PRO159 |
| B | THR160 |
| B | HIS163 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24412362","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
