2HO4
Crystal Structure of Protein from Mouse Mm.236127
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 260 |
| Chain | Residue |
| A | ASP13 |
| A | ASN15 |
| A | ASP204 |
| A | HOH446 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| B | HOH461 |
| B | ASP13 |
| B | ASN15 |
| B | ASP204 |
| B | PO4401 |
| B | HOH459 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 401 |
| Chain | Residue |
| B | ASP13 |
| B | ASN15 |
| B | THR46 |
| B | ASN47 |
| B | LYS179 |
| B | MG301 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 402 |
| Chain | Residue |
| A | ARG207 |
| A | LYS235 |
| A | HOH460 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 B 403 |
| Chain | Residue |
| B | ARG207 |
| B | LYS235 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 404 |
| Chain | Residue |
| A | ASN47 |
| A | THR48 |
| A | THR49 |
| A | LYS50 |
| A | GLU51 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 B 405 |
| Chain | Residue |
| B | LYS50 |
| B | ARG97 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PO4 A 406 |
| Chain | Residue |
| A | LYS182 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 50 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of protein from mouse mm.236127.","authoringGroup":["Center for eukaryotic structural genomics (CESG)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
