MolNFT v1 · #40718 · protein

P53 tetramerization domain mutant Y327S T329G Q331G

2J11 · Cellular tumor antigen P53: “P53 tetramerization domain mutant Y327S T329G Q331G”. Solution nmr, 2 pockets (best druggability 0.44). MolNFT v1 #40718 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2J11
Type: protein
Length: 124 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular tumor antigen P53
UniProt: P04637
Pockets: 2 · best druggability 0.44

Structure

solution nmr · 1 distinct chain · 65% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Cellular tumor antigen P53	protein	31	65% helix, 10% strand	P04637

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	108	0.44	0.78	19	empty
2	75	0.32	0.74	11	empty

Interfaces

6 interfaces between chains.

A–B · 943 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 916 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 311 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 306 Å² buried · 1 hydrogen bond · protein-protein
A–C · 95 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2J11 · p53 tetramerization domain mutant Y327S T329G Q331G · the same entry in another collection · chain A against A, TM-score 1.00

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 P04637
Elsewhere: RCSB PDB 2J11 · PDBe 2J11 · UniProt P04637

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