5AE3
Ether Lipid-Generating Enzyme AGPS in complex with antimycin A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005777 | cellular_component | peroxisome |
A | 0005778 | cellular_component | peroxisomal membrane |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008609 | molecular_function | alkylglycerone-phosphate synthase activity |
A | 0008610 | biological_process | lipid biosynthetic process |
A | 0008611 | biological_process | ether lipid biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016740 | molecular_function | transferase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071949 | molecular_function | FAD binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0005777 | cellular_component | peroxisome |
B | 0005778 | cellular_component | peroxisomal membrane |
B | 0006629 | biological_process | lipid metabolic process |
B | 0008609 | molecular_function | alkylglycerone-phosphate synthase activity |
B | 0008610 | biological_process | lipid biosynthetic process |
B | 0008611 | biological_process | ether lipid biosynthetic process |
B | 0016020 | cellular_component | membrane |
B | 0016740 | molecular_function | transferase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0071949 | molecular_function | FAD binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0005777 | cellular_component | peroxisome |
C | 0005778 | cellular_component | peroxisomal membrane |
C | 0006629 | biological_process | lipid metabolic process |
C | 0008609 | molecular_function | alkylglycerone-phosphate synthase activity |
C | 0008610 | biological_process | lipid biosynthetic process |
C | 0008611 | biological_process | ether lipid biosynthetic process |
C | 0016020 | cellular_component | membrane |
C | 0016740 | molecular_function | transferase activity |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0071949 | molecular_function | FAD binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0005777 | cellular_component | peroxisome |
D | 0005778 | cellular_component | peroxisomal membrane |
D | 0006629 | biological_process | lipid metabolic process |
D | 0008609 | molecular_function | alkylglycerone-phosphate synthase activity |
D | 0008610 | biological_process | lipid biosynthetic process |
D | 0008611 | biological_process | ether lipid biosynthetic process |
D | 0016020 | cellular_component | membrane |
D | 0016740 | molecular_function | transferase activity |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AWB A 800 |
Chain | Residue |
A | PHE128 |
A | ILE511 |
A | MET514 |
A | GLY518 |
A | LEU562 |
A | ARG566 |
A | TYR580 |
A | HOH2121 |
A | HOH2162 |
A | PHE136 |
A | ARG419 |
A | MET421 |
A | GLN425 |
A | PHE428 |
A | THR467 |
A | GLY504 |
A | TYR505 |
site_id | AC2 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD A 999 |
Chain | Residue |
A | TRP96 |
A | PRO234 |
A | ILE235 |
A | GLY236 |
A | GLY237 |
A | GLY238 |
A | THR239 |
A | SER240 |
A | VAL241 |
A | GLY244 |
A | LEU245 |
A | PRO302 |
A | ASP303 |
A | SER304 |
A | SER308 |
A | THR309 |
A | GLY312 |
A | TRP313 |
A | SER315 |
A | THR316 |
A | ALA318 |
A | SER319 |
A | GLU368 |
A | GLY369 |
A | GLY372 |
A | VAL373 |
A | ILE374 |
A | ALA512 |
A | HIS616 |
A | ASN654 |
A | ASN656 |
A | HOH2042 |
A | HOH2045 |
A | HOH2071 |
A | HOH2077 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AWB B 800 |
Chain | Residue |
B | PHE128 |
B | TRP131 |
B | PHE136 |
B | ARG419 |
B | MET421 |
B | GLN425 |
B | PHE428 |
B | THR467 |
B | GLY504 |
B | TYR505 |
B | ILE511 |
B | MET514 |
B | ARG515 |
B | GLY518 |
B | GLU526 |
B | ARG566 |
B | TYR580 |
B | HOH2092 |
site_id | AC4 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD B 999 |
Chain | Residue |
B | HIS616 |
B | ASN654 |
B | ASN656 |
B | HOH2044 |
B | HOH2047 |
B | HOH2062 |
B | HOH2064 |
B | HOH2068 |
B | TRP96 |
B | HIS189 |
B | PRO234 |
B | ILE235 |
B | GLY236 |
B | GLY237 |
B | GLY238 |
B | THR239 |
B | SER240 |
B | VAL241 |
B | GLY244 |
B | LEU245 |
B | PRO302 |
B | ASP303 |
B | SER304 |
B | SER308 |
B | THR309 |
B | GLY312 |
B | TRP313 |
B | SER315 |
B | THR316 |
B | ALA318 |
B | SER319 |
B | GLU368 |
B | GLY369 |
B | GLY372 |
B | VAL373 |
B | ILE374 |
B | ALA512 |
site_id | AC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE AWB C 800 |
Chain | Residue |
C | PHE136 |
C | MET421 |
C | GLN425 |
C | PHE428 |
C | ARG503 |
C | GLY504 |
C | TYR505 |
C | LEU506 |
C | LEU507 |
C | ILE511 |
C | MET514 |
C | GLY518 |
C | ILE523 |
C | GLY525 |
C | GLU526 |
C | ARG566 |
C | TYR580 |
C | HOH2126 |
C | HOH2145 |
site_id | AC6 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD C 999 |
Chain | Residue |
C | TRP96 |
C | PRO234 |
C | ILE235 |
C | GLY236 |
C | GLY237 |
C | GLY238 |
C | THR239 |
C | SER240 |
C | GLY244 |
C | LEU245 |
C | PRO302 |
C | ASP303 |
C | SER304 |
C | SER308 |
C | THR309 |
C | GLY312 |
C | TRP313 |
C | SER315 |
C | THR316 |
C | ALA318 |
C | SER319 |
C | GLU368 |
C | GLY369 |
C | GLY372 |
C | VAL373 |
C | ILE374 |
C | ALA512 |
C | HIS616 |
C | ASN656 |
C | HOH2047 |
C | HOH2051 |
C | HOH2074 |
C | HOH2075 |
C | HOH2078 |
site_id | AC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE AWB D 800 |
Chain | Residue |
D | TRP131 |
D | PHE136 |
D | MET421 |
D | GLN425 |
D | PHE428 |
D | GLY504 |
D | TYR505 |
D | LEU506 |
D | LEU507 |
D | ILE511 |
D | MET514 |
D | GLY518 |
D | ILE523 |
D | GLU526 |
D | SER527 |
D | LEU562 |
D | ARG566 |
D | TYR580 |
D | HOH2103 |
site_id | AC8 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD D 999 |
Chain | Residue |
D | TRP96 |
D | HIS189 |
D | PRO234 |
D | ILE235 |
D | GLY236 |
D | GLY237 |
D | GLY238 |
D | THR239 |
D | SER240 |
D | VAL241 |
D | GLY244 |
D | LEU245 |
D | PRO302 |
D | ASP303 |
D | SER304 |
D | SER308 |
D | THR309 |
D | GLY312 |
D | TRP313 |
D | SER315 |
D | THR316 |
D | ALA318 |
D | SER319 |
D | GLU368 |
D | GLY369 |
D | GLY372 |
D | VAL373 |
D | ILE374 |
D | ALA512 |
D | HIS616 |
D | ASN654 |
D | ASN656 |
D | HOH2038 |
D | HOH2040 |
D | HOH2044 |
D | HOH2066 |
D | HOH2067 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 1659 |
Chain | Residue |
C | LYS380 |
D | LYS323 |
D | TYR571 |
D | ASP572 |
D | HOH2071 |
D | HOH2120 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1659 |
Chain | Residue |
A | LYS323 |
A | TYR571 |
A | ASP572 |
A | HOH2080 |
A | HOH2141 |
B | LYS380 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 1659 |
Chain | Residue |
A | LYS380 |
B | LYS323 |
B | TYR571 |
B | ASP572 |
B | HOH2105 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:23112191 |
Chain | Residue | Details |
A | TYR578 | |
B | TYR578 | |
C | TYR578 | |
D | TYR578 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23112191 |
Chain | Residue | Details |
A | PRO234 | |
B | ARG515 | |
C | PRO234 | |
C | ASP303 | |
C | THR316 | |
C | GLU368 | |
C | ARG515 | |
D | PRO234 | |
D | ASP303 | |
D | THR316 | |
D | GLU368 | |
A | ASP303 | |
D | ARG515 | |
A | THR316 | |
A | GLU368 | |
A | ARG515 | |
B | PRO234 | |
B | ASP303 | |
B | THR316 | |
B | GLU368 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Important for enzyme activity => ECO:0000269|PubMed:10692424, ECO:0000269|PubMed:23112191 |
Chain | Residue | Details |
A | ARG419 | |
B | ARG419 | |
C | ARG419 | |
D | ARG419 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O00116 |
Chain | Residue | Details |
A | SER65 | |
B | SER65 | |
C | SER65 | |
D | SER65 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O00116 |
Chain | Residue | Details |
A | THR74 | |
B | THR74 | |
C | THR74 | |
D | THR74 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O00116 |
Chain | Residue | Details |
A | LYS102 | |
A | LYS347 | |
B | LYS102 | |
B | LYS347 | |
C | LYS102 | |
C | LYS347 | |
D | LYS102 | |
D | LYS347 |