4XIZ
Structure of a phospholipid trafficking complex with substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0006869 | biological_process | lipid transport |
| A | 0008289 | molecular_function | lipid binding |
| A | 0015914 | biological_process | phospholipid transport |
| A | 0032048 | biological_process | cardiolipin metabolic process |
| A | 0120010 | biological_process | intermembrane phospholipid transfer |
| A | 1990050 | molecular_function | phosphatidic acid transfer activity |
| A | 2001247 | biological_process | positive regulation of phosphatidylcholine biosynthetic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0006869 | biological_process | lipid transport |
| B | 0008289 | molecular_function | lipid binding |
| B | 0015914 | biological_process | phospholipid transport |
| B | 0032048 | biological_process | cardiolipin metabolic process |
| B | 0120010 | biological_process | intermembrane phospholipid transfer |
| B | 1990050 | molecular_function | phosphatidic acid transfer activity |
| B | 2001247 | biological_process | positive regulation of phosphatidylcholine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue LPP A 201 |
| Chain | Residue |
| A | ARG25 |
| A | MET104 |
| A | VAL106 |
| A | GLU107 |
| A | GLU108 |
| A | THR110 |
| A | TYR112 |
| A | SER125 |
| A | TRP144 |
| A | LYS148 |
| A | ASN152 |
| A | TYR26 |
| A | LYS155 |
| A | SER156 |
| A | HOH346 |
| A | HOH385 |
| A | HOH390 |
| A | HOH397 |
| A | SER31 |
| A | VAL34 |
| A | LYS58 |
| A | ILE78 |
| A | THR95 |
| A | ARG96 |
| A | ASN97 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue LPP B 201 |
| Chain | Residue |
| B | TYR26 |
| B | LYS58 |
| B | ILE78 |
| B | THR95 |
| B | ARG96 |
| B | ASN97 |
| B | HIS100 |
| B | ILE103 |
| B | VAL106 |
| B | GLU108 |
| B | ALA123 |
| B | SER125 |
| B | TRP144 |
| B | LYS148 |
| B | ASN152 |
| B | VAL153 |
| B | SER156 |
| B | HOH411 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 158 |
| Details | Region: {"description":"Required for mitochondrial targeting","evidences":[{"source":"PubMed","id":"16754953","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26235513","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26071601","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26071601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26235513","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 100 |
| Details | Domain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Motif: {"description":"Cx9C motif 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Motif: {"description":"Cx9C motif 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
