1A2O
STRUCTURAL BASIS FOR METHYLESTERASE CHEB REGULATION BY A PHOSPHORYLATION-ACTIVATED DOMAIN
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000156 | molecular_function | phosphorelay response regulator activity |
A | 0000160 | biological_process | phosphorelay signal transduction system |
A | 0005737 | cellular_component | cytoplasm |
A | 0006482 | biological_process | protein demethylation |
A | 0006935 | biological_process | chemotaxis |
A | 0008984 | molecular_function | protein-glutamate methylesterase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0018277 | biological_process | protein deamination |
A | 0050568 | molecular_function | protein-glutamine glutaminase activity |
B | 0000156 | molecular_function | phosphorelay response regulator activity |
B | 0000160 | biological_process | phosphorelay signal transduction system |
B | 0005737 | cellular_component | cytoplasm |
B | 0006482 | biological_process | protein demethylation |
B | 0006935 | biological_process | chemotaxis |
B | 0008984 | molecular_function | protein-glutamate methylesterase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0018277 | biological_process | protein deamination |
B | 0050568 | molecular_function | protein-glutamine glutaminase activity |
Functional Information from PDB Data
site_id | ESE |
Number of Residues | 3 |
Details | ESTERASE CATALYTIC TRIAD |
Chain | Residue |
A | SER164 |
A | HIS190 |
A | ASP286 |
site_id | PON |
Number of Residues | 1 |
Details | PHOSPHORYLATION SITE |
Chain | Residue |
A | ASP56 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000305|PubMed:7608974 |
Chain | Residue | Details |
A | SER164 | |
A | HIS190 | |
A | ASP286 | |
B | SER164 | |
B | HIS190 | |
B | ASP286 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:9465023 |
Chain | Residue | Details |
A | ASP56 | |
B | ASP56 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1chd |
Chain | Residue | Details |
A | ASP286 | |
A | SER164 | |
A | MET283 | |
A | THR165 | |
A | HIS190 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1chd |
Chain | Residue | Details |
B | ASP286 | |
B | SER164 | |
B | MET283 | |
B | THR165 | |
B | HIS190 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 337 |
Chain | Residue | Details |
A | SER164 | activator, covalently attached, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | THR165 | electrostatic stabiliser, hydrogen bond donor |
A | HIS190 | activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
A | MET283 | electrostatic stabiliser, hydrogen bond donor |
A | ASP286 | electrostatic stabiliser, hydrogen bond acceptor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 337 |
Chain | Residue | Details |
B | SER164 | activator, covalently attached, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | THR165 | electrostatic stabiliser, hydrogen bond donor |
B | HIS190 | activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
B | MET283 | electrostatic stabiliser, hydrogen bond donor |
B | ASP286 | electrostatic stabiliser, hydrogen bond acceptor |