6SQP
Crystal structure of Cat MDM2-S429E RING domain homodimer
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0051726 | biological_process | regulation of cell cycle |
| A | 0061630 | molecular_function | ubiquitin protein ligase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0051726 | biological_process | regulation of cell cycle |
| B | 0061630 | molecular_function | ubiquitin protein ligase activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0043066 | biological_process | negative regulation of apoptotic process |
| C | 0051726 | biological_process | regulation of cell cycle |
| C | 0061630 | molecular_function | ubiquitin protein ligase activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0043066 | biological_process | negative regulation of apoptotic process |
| D | 0051726 | biological_process | regulation of cell cycle |
| D | 0061630 | molecular_function | ubiquitin protein ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | CYS438 |
| A | CYS441 |
| A | CYS461 |
| A | CYS464 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | HIS452 |
| A | HIS457 |
| A | CYS475 |
| A | CYS478 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | ARG479 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| B | CYS438 |
| B | CYS441 |
| B | ARG444 |
| B | CYS461 |
| B | CYS464 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 502 |
| Chain | Residue |
| B | HIS452 |
| B | HIS457 |
| B | CYS475 |
| B | CYS478 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 501 |
| Chain | Residue |
| C | CYS438 |
| C | CYS441 |
| C | CYS461 |
| C | CYS464 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 502 |
| Chain | Residue |
| C | HIS452 |
| C | HIS457 |
| C | CYS475 |
| C | CYS478 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| D | CYS438 |
| D | CYS441 |
| D | CYS461 |
| D | CYS464 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 502 |
| Chain | Residue |
| D | HIS452 |
| D | HIS457 |
| D | CYS475 |
| D | CYS478 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 D 503 |
| Chain | Residue |
| B | ASN472 |
| D | ARG444 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 164 |
| Details | Zinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Motif: {"description":"Nucleolar localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by ATM","evidences":[{"source":"UniProtKB","id":"Q00987","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
