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The tetramerization domain of human P73

Analyse The tetramerization domain of human P73 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KBY
Type: protein
Length: 192 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor protein P73
UniProt: O15350
Pockets: 2 · best druggability 0.31

Structure

solution nmr · 1 distinct chain · 58% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Tumor protein P73	protein	48	58% helix, 15% strand	O15350

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.31	0.75	17	empty
2	63	0.29	0.74	17	empty

Interfaces

6 interfaces between chains.

A–B · 1306 Å² buried · 28 hydrogen bonds · protein-protein
C–D · 1306 Å² buried · 28 hydrogen bonds · protein-protein
A–C · 1035 Å² buried · 9 hydrogen bonds · protein-protein
B–D · 1035 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 502 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2KBY · The Tetramerization Domain of Human p73 · 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 A against A, TM-score 0.72

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 O15350
Elsewhere: RCSB PDB 2KBY · PDBe 2KBY · UniProt O15350

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