Research workbench

Structure of the human mdmx protein bound to the P53 tumor suppressor transactivation domain

Analyse Structure of the human mdmx protein bound to the P53 tumor suppressor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DAB
Type: protein
Length: 394 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MDM4 protein; Cellular tumor antigen P53
UniProt: O15151, P04637
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 6 distinct chains · 46% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, G	MDM4 protein	protein	88	44% helix, 16% strand	O15151
B	Cellular tumor antigen P53	protein	12	50% helix, 0% strand	P04637
C, E	MDM4 protein	protein	86	45% helix, 13% strand	O15151
D	Cellular tumor antigen P53	protein	11	45% helix, 0% strand	P04637
F	Cellular tumor antigen P53	protein	12	50% helix, 0% strand	P04637
H	Cellular tumor antigen P53	protein	11	55% helix, 0% strand	P04637

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	417	0.67	0.80	35	empty
2	427	0.64	0.78	51	empty
3	184	0.52	0.79	33	empty

Interfaces

9 interfaces between chains.

A–B · 595 Å² buried · 5 hydrogen bonds · protein-protein
G–H · 567 Å² buried · 4 hydrogen bonds · protein-protein
E–F · 543 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 486 Å² buried · 2 hydrogen bonds · protein-protein
E–G · 336 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3DAB · Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation… · the same entry in another collection · chain H against H, TM-score 1.00
O15151 · AlphaFold monomer V2.0 prediction for protein MDM4 (O15151) · a predicted model of the same protein · chain A against A, TM-score 0.95

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O15151
Every structure of UniProt P04637
Elsewhere: RCSB PDB 3DAB · PDBe 3DAB · UniProt O15151 · UniProt P04637

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.