Research workbench

Crystal structure of P63 SAM in complex with darpin A5

Analyse Crystal structure of P63 SAM in complex with darpin A5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7Z72
Type: protein
Length: 222 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 9 of tumor protein 63; Darpin A5
UniProt: Q9H3D4
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isoform 9 of tumor protein 63	protein	65	66% helix, 3% strand	Q9H3D4
B	Darpin A5	protein	157	55% helix, 0% strand	—

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · chains B

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

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	116	0.40	0.75	17	empty
2	86	0.31	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 908 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

7Z72 · Crystal structure of p63 SAM in complex with darpin A5 · the same entry in another collection · chain A against A, TM-score 1.00
Q9H3D4 · AlphaFold monomer V2.0 prediction for tumor protein 63 (Q9H3D4) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9H3D4
Elsewhere: RCSB PDB 7Z72 · PDBe 7Z72 · UniProt Q9H3D4

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