2F6U
Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with citrate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0002094 | molecular_function | polyprenyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006650 | biological_process | glycerophospholipid metabolic process |
A | 0008654 | biological_process | phospholipid biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0046474 | biological_process | glycerophospholipid biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0047294 | molecular_function | phosphoglycerol geranylgeranyltransferase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0002094 | molecular_function | polyprenyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006650 | biological_process | glycerophospholipid metabolic process |
B | 0008654 | biological_process | phospholipid biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
B | 0046474 | biological_process | glycerophospholipid biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0047294 | molecular_function | phosphoglycerol geranylgeranyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CIT A 3001 |
Chain | Residue |
A | HOH5 |
A | GLY1195 |
A | ILE1213 |
A | GLY1215 |
A | ASN1216 |
A | HOH10 |
A | HOH258 |
A | LYS1011 |
A | TYR1165 |
A | GLU1167 |
A | SER1169 |
A | GLY1170 |
A | GLY1193 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CIT B 3002 |
Chain | Residue |
B | HOH9 |
B | HOH32 |
B | HOH280 |
B | LYS2011 |
B | TYR2165 |
B | GLU2167 |
B | SER2169 |
B | GLY2170 |
B | GLY2193 |
B | GLY2194 |
B | GLY2195 |
B | ILE2213 |
B | GLY2215 |
B | ASN2216 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AVADSGTDAVMI |
Chain | Residue | Details |
A | ALA1025-ILE1036 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:16377641, ECO:0007744|PDB:2F6X |
Chain | Residue | Details |
B | LYS2011 | |
B | TYR2165 | |
B | GLY2195 | |
B | GLY2215 | |
A | LYS1011 | |
A | TYR1165 | |
A | GLY1195 | |
A | GLY1215 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00112 |
Chain | Residue | Details |
B | ASP2013 | |
B | THR2039 | |
A | ASP1013 | |
A | THR1039 |