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Structure of complex of MDM2(3-109) and P73 TAD(10-25)

Analyse Structure of complex of MDM2(3-109) and P73 TAD(10-25) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MPS
Type: protein
Length: 123 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase MDM2; Tumor protein P73
EC: 6.3.2.-
UniProt: Q00987, O15350
Pockets: 1 · best druggability 0.36

Structure

solution nmr · 2 distinct chains · 36% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase MDM2 (EC 6.3.2.-)	protein	107	36% helix, 7% strand	Q00987
B	Tumor protein P73	protein	16	38% helix, 0% strand	O15350

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.36	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 726 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2MPS · Structure of complex of MDM2(3-109) and P73 TAD(10-25) · the same entry in another collection · chain A against A, TM-score 1.00
O15350 · AlphaFold monomer V2.0 prediction for tumor protein P73 (O15350) · a predicted model of the same protein · chain B against A, TM-score 0.35

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 Q00987
Every structure of UniProt O15350
Elsewhere: RCSB PDB 2MPS · PDBe 2MPS · UniProt Q00987 · UniProt O15350

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