2VJE
Crystal Structure of the MDM2-MDMX RING Domain Heterodimer
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 | 0043066 | biological_process | negative regulation of apoptotic process |
B | 0051726 | biological_process | regulation of cell cycle |
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 | 0043066 | biological_process | negative regulation of apoptotic process |
D | 0051726 | biological_process | regulation of cell cycle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A1492 |
Chain | Residue |
A | CYS438 |
A | CYS441 |
A | CYS461 |
A | CYS464 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A1493 |
Chain | Residue |
A | HIS452 |
A | HIS457 |
A | CYS475 |
A | CYS478 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B1491 |
Chain | Residue |
B | CYS440 |
B | CYS460 |
B | CYS463 |
B | CYS437 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B1492 |
Chain | Residue |
B | HIS451 |
B | HIS456 |
B | CYS474 |
B | CYS477 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C1492 |
Chain | Residue |
C | CYS438 |
C | CYS441 |
C | CYS461 |
C | CYS464 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C1493 |
Chain | Residue |
C | HIS452 |
C | HIS457 |
C | CYS475 |
C | CYS478 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D1491 |
Chain | Residue |
D | CYS437 |
D | CYS440 |
D | CYS460 |
D | CYS463 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D1492 |
Chain | Residue |
D | HIS451 |
D | HIS456 |
D | CYS474 |
D | CYS477 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FLC D1493 |
Chain | Residue |
D | LYS442 |
D | ARG443 |
D | HIS462 |
D | ARG466 |
D | HOH2017 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D1494 |
Chain | Residue |
B | SER473 |
D | ARG453 |
D | HOH2029 |
D | HOH2030 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 82 |
Details | ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175 |
Chain | Residue | Details |
B | CYS437-LYS478 | |
C | PRO474 | |
D | CYS437-LYS478 | |
A | HIS452 | |
A | LYS470 | |
A | PRO474 | |
C | PRO431 | |
C | ILE440 | |
C | HIS452 | |
C | LYS470 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by ATM => ECO:0000269|PubMed:19816404 |
Chain | Residue | Details |
A | CYS464 | |
C | CYS464 |