3B7Q
Crystal Structure of Yeast Sec14 Homolog Sfh1 in Complex with Phosphatidylcholine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0006892 | biological_process | post-Golgi vesicle-mediated transport |
| A | 0008150 | biological_process | biological_process |
| A | 0008526 | molecular_function | phosphatidylinositol transfer activity |
| A | 0015914 | biological_process | phospholipid transport |
| A | 0031210 | molecular_function | phosphatidylcholine binding |
| A | 0035091 | molecular_function | phosphatidylinositol binding |
| A | 0120009 | biological_process | intermembrane lipid transfer |
| B | 0005634 | cellular_component | nucleus |
| B | 0006892 | biological_process | post-Golgi vesicle-mediated transport |
| B | 0008150 | biological_process | biological_process |
| B | 0008526 | molecular_function | phosphatidylinositol transfer activity |
| B | 0015914 | biological_process | phospholipid transport |
| B | 0031210 | molecular_function | phosphatidylcholine binding |
| B | 0035091 | molecular_function | phosphatidylinositol binding |
| B | 0120009 | biological_process | intermembrane lipid transfer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 311 |
| Chain | Residue |
| A | PHE221 |
| A | GLY222 |
| A | PHE223 |
| A | SER224 |
| A | HOH463 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 312 |
| Chain | Residue |
| A | LYS95 |
| A | ASN301 |
| A | GLY304 |
| A | HOH428 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 313 |
| Chain | Residue |
| A | GLY246 |
| A | SER247 |
| A | SER248 |
| A | HOH420 |
| A | HOH504 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 6PL A 314 |
| Chain | Residue |
| A | TYR109 |
| A | TYR113 |
| A | TYR124 |
| A | LEU128 |
| A | ILE131 |
| A | MET136 |
| A | TYR137 |
| A | THR140 |
| A | THR141 |
| A | MET145 |
| A | TYR153 |
| A | SER175 |
| A | THR177 |
| A | TYR195 |
| A | ILE196 |
| A | MET211 |
| A | THR238 |
| A | HOH350 |
| A | HOH365 |
| A | HOH386 |
| A | HOH417 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 315 |
| Chain | Residue |
| A | VAL271 |
| A | LEU272 |
| A | PRO275 |
| A | ASP277 |
| A | HOH448 |
| A | HOH506 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 311 |
| Chain | Residue |
| B | PHE221 |
| B | GLY222 |
| B | SER224 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 312 |
| Chain | Residue |
| B | LYS95 |
| B | ASN301 |
| B | GLY304 |
| B | LYS305 |
| B | HOH349 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 313 |
| Chain | Residue |
| B | GLY246 |
| B | SER247 |
| B | SER248 |
| B | HOH484 |
| B | HOH487 |
| B | HOH496 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 6PL B 314 |
| Chain | Residue |
| B | TYR109 |
| B | TYR113 |
| B | TYR124 |
| B | LEU128 |
| B | ILE131 |
| B | LEU133 |
| B | TYR137 |
| B | MET145 |
| B | LEU149 |
| B | GLU152 |
| B | TYR153 |
| B | SER175 |
| B | THR177 |
| B | ALA189 |
| B | TYR195 |
| B | ILE196 |
| B | ARG210 |
| B | MET211 |
| B | PHE214 |
| B | HOH365 |
| B | HOH427 |
| B | HOH448 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 346 |
| Details | Domain: {"description":"CRAL-TRIO","evidences":[{"source":"PROSITE-ProRule","id":"PRU00056","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
