7RXZ
human Hsp90_MC domain structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0051082 | molecular_function | unfolded protein binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006457 | biological_process | protein folding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0051082 | molecular_function | unfolded protein binding |
| F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG400 | |
| B | ARG400 | |
| C | ARG400 | |
| D | ARG400 | |
| E | ARG400 | |
| F | ARG400 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07901 |
| Chain | Residue | Details |
| A | TYR313 | |
| E | TYR492 | |
| F | TYR313 | |
| F | TYR492 | |
| A | TYR492 | |
| B | TYR313 | |
| B | TYR492 | |
| C | TYR313 | |
| C | TYR492 | |
| D | TYR313 | |
| D | TYR492 | |
| E | TYR313 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS443 | |
| C | LYS458 | |
| C | LYS489 | |
| C | LYS585 | |
| D | LYS443 | |
| D | LYS458 | |
| D | LYS489 | |
| D | LYS585 | |
| E | LYS443 | |
| E | LYS458 | |
| E | LYS489 | |
| A | LYS458 | |
| E | LYS585 | |
| F | LYS443 | |
| F | LYS458 | |
| F | LYS489 | |
| F | LYS585 | |
| A | LYS489 | |
| A | LYS585 | |
| B | LYS443 | |
| B | LYS458 | |
| B | LYS489 | |
| B | LYS585 | |
| C | LYS443 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P82995 |
| Chain | Residue | Details |
| A | SER453 | |
| B | SER453 | |
| C | SER453 | |
| D | SER453 | |
| E | SER453 | |
| F | SER453 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER476 | |
| E | SER641 | |
| F | SER476 | |
| F | SER641 | |
| A | SER641 | |
| B | SER476 | |
| B | SER641 | |
| C | SER476 | |
| C | SER641 | |
| D | SER476 | |
| D | SER641 | |
| E | SER476 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:15937123 |
| Chain | Residue | Details |
| A | CYS598 | |
| B | CYS598 | |
| C | CYS598 | |
| D | CYS598 | |
| E | CYS598 | |
| F | CYS598 |
