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Human P53 core domain mutant V157F

Analyse Human P53 core domain mutant V157F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KVP
Type: protein
Length: 777 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular tumor antigen P53
UniProt: P04637
Ligands: ZN
Pockets: 9 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Cellular tumor antigen P53	protein	194	8% helix, 34% strand	P04637
C	Cellular tumor antigen P53	protein	195	10% helix, 33% strand	P04637

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	280	0.57	0.77	37	empty
2	128	0.40	0.75	18	empty
3	88	0.38	0.76	19	empty
4	94	0.38	0.76	20	empty
5	106	0.37	0.74	21	empty

Interfaces

2 interfaces between chains.

B–D · 512 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 299 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4KVP · Human p53 Core Domain Mutant V157F · 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 4KVP · PDBe 4KVP · UniProt P04637

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