4NR2
Crystal structure of STK4 (MST1) SARAH domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0007165 | biological_process | signal transduction |
| A | 0051262 | biological_process | protein tetramerization |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0007165 | biological_process | signal transduction |
| B | 0051262 | biological_process | protein tetramerization |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0007165 | biological_process | signal transduction |
| C | 0051262 | biological_process | protein tetramerization |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0007165 | biological_process | signal transduction |
| D | 0051262 | biological_process | protein tetramerization |
| E | 0004674 | molecular_function | protein serine/threonine kinase activity |
| E | 0007165 | biological_process | signal transduction |
| E | 0051262 | biological_process | protein tetramerization |
| F | 0004674 | molecular_function | protein serine/threonine kinase activity |
| F | 0007165 | biological_process | signal transduction |
| F | 0051262 | biological_process | protein tetramerization |
| G | 0004674 | molecular_function | protein serine/threonine kinase activity |
| G | 0007165 | biological_process | signal transduction |
| G | 0051262 | biological_process | protein tetramerization |
| H | 0004674 | molecular_function | protein serine/threonine kinase activity |
| H | 0007165 | biological_process | signal transduction |
| H | 0051262 | biological_process | protein tetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 501 |
| Chain | Residue |
| A | LEU451 |
| A | ASP452 |
| A | MET455 |
| A | HOH642 |
| B | ARG470 |
| B | EDO501 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | LYS465 |
| B | GLU458 |
| E | PHE435 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | ARG470 |
| A | HOH603 |
| A | HOH638 |
| B | ASP452 |
| B | MET455 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | LYS446 |
| A | ARG447 |
| A | ALA450 |
| A | HOH602 |
| E | PRO453 |
| E | MET454 |
| E | GLN457 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| A | ASP452 |
| A | EDO501 |
| A | HOH642 |
| B | ARG470 |
| D | LEU449 |
| D | ASP452 |
| D | PRO453 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 501 |
| Chain | Residue |
| A | HOH635 |
| C | ARG470 |
| D | LEU451 |
| D | ASP452 |
| D | MET455 |
| D | HOH507 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO E 501 |
| Chain | Residue |
| A | MET454 |
| E | MET0 |
| E | ARG447 |
| E | HOH620 |
| F | LYS469 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO F 501 |
| Chain | Residue |
| F | PHE435 |
| F | ARG463 |
| F | GLN464 |
| F | GLN467 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO H 501 |
| Chain | Residue |
| C | MET454 |
| D | HOH513 |
| G | LYS469 |
| G | HOH517 |
| H | MET0 |
| H | ARG447 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO H 502 |
| Chain | Residue |
| G | ARG470 |
| H | LEU451 |
| H | ASP452 |
| H | MET455 |
| H | HOH605 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9JI11 |
| Chain | Residue | Details |
| A | TYR433 | |
| B | TYR433 | |
| C | TYR433 | |
| D | TYR433 | |
| E | TYR433 | |
| F | TYR433 | |
| G | TYR433 | |
| H | TYR433 |
