1FXW
CRYSTAL STRUCTURE OF THE RECOMBINANT ALPHA1/ALPHA2 CATALYTIC HETERODIMER OF BOVINE BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003847 | molecular_function | 1-alkyl-2-acetylglycerophosphocholine esterase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0007283 | biological_process | spermatogenesis |
| A | 0008247 | cellular_component | 1-alkyl-2-acetylglycerophosphocholine esterase complex |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0047179 | molecular_function | platelet-activating factor acetyltransferase activity |
| F | 0001650 | cellular_component | fibrillar center |
| F | 0003847 | molecular_function | 1-alkyl-2-acetylglycerophosphocholine esterase activity |
| F | 0005730 | cellular_component | nucleolus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0007283 | biological_process | spermatogenesis |
| F | 0008247 | cellular_component | 1-alkyl-2-acetylglycerophosphocholine esterase complex |
| F | 0016042 | biological_process | lipid catabolic process |
| F | 0016239 | biological_process | positive regulation of macroautophagy |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0042803 | molecular_function | protein homodimerization activity |
| F | 0046982 | molecular_function | protein heterodimerization activity |
| F | 0047179 | molecular_function | platelet-activating factor acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 238 |
| Chain | Residue |
| A | SER47 |
| A | GLY74 |
| A | ASN104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| F | SER48 | |
| F | ASP193 | |
| F | HIS196 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68402 |
| Chain | Residue | Details |
| F | SER2 | |
| F | SER64 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q61206 |
| Chain | Residue | Details |
| F | THR220 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bwp |
| Chain | Residue | Details |
| A | ASP192 | |
| A | ASN104 | |
| A | SER47 | |
| A | HIS195 | |
| A | GLY74 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bwp |
| Chain | Residue | Details |
| F | SER48 | |
| F | GLY75 | |
| F | ASP193 | |
| F | ASN105 | |
| F | HIS196 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 94 |
| Chain | Residue | Details |
| A | SER47 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY74 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN104 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP192 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS195 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
