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 | 0045332 | biological_process | phospholipid translocation |
A | 0120009 | biological_process | intermembrane lipid 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 | 0045332 | biological_process | phospholipid translocation |
B | 0120009 | biological_process | intermembrane lipid 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 | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26235513 |
Chain | Residue | Details |
A | TYR26 | |
A | LYS58 | |
B | TYR26 | |
B | LYS58 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26071601 |
Chain | Residue | Details |
A | LYS148 | |
B | LYS148 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26071601, ECO:0000269|PubMed:26235513 |
Chain | Residue | Details |
A | ASN152 | |
B | ASN152 |