3FXM
Crystal Structure of Human Protein phosphatase 1A (PPM1A) Bound with Citrate at 10 mM of Mn2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0006499 | biological_process | N-terminal protein myristoylation |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030512 | biological_process | negative regulation of transforming growth factor beta receptor signaling pathway |
| A | 0033192 | molecular_function | calmodulin-dependent protein phosphatase activity |
| A | 0043122 | biological_process | regulation of canonical NF-kappaB signal transduction |
| A | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| A | 0043124 | biological_process | negative regulation of canonical NF-kappaB signal transduction |
| A | 0043169 | molecular_function | cation binding |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051726 | biological_process | regulation of cell cycle |
| A | 0070412 | molecular_function | R-SMAD binding |
| A | 0090263 | biological_process | positive regulation of canonical Wnt signaling pathway |
| A | 1901223 | biological_process | negative regulation of non-canonical NF-kappaB signal transduction |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 391 |
| Chain | Residue |
| A | ASP60 |
| A | ASP239 |
| A | ASP282 |
| A | HOH435 |
| A | HOH553 |
| A | HOH618 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 392 |
| Chain | Residue |
| A | HOH416 |
| A | HOH552 |
| A | HOH553 |
| A | ASP60 |
| A | GLY61 |
| A | HOH402 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 393 |
| Chain | Residue |
| A | ASN188 |
| A | LEU214 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC A 394 |
| Chain | Residue |
| A | ARG33 |
| A | GLU37 |
| A | HIS62 |
| A | ALA63 |
| A | ARG186 |
| A | GLU300 |
| A | LYS303 |
| A | HOH416 |
| A | HOH552 |
Functional Information from PROSITE/UniProt
| site_id | PS01032 |
| Number of Residues | 9 |
| Details | PPM_1 PPM-type phosphatase domain signature. FFAVYDGHA |
| Chain | Residue | Details |
| A | PHE55-ALA63 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 268 |
| Details | Domain: {"description":"PPM-type phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01082","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9003755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A6Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"N-myristoyl glycine","evidences":[{"source":"PubMed","id":"20213681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
