MolNFT v1 · #61147 · protein

Crystal structure a TP53-induced glycolysis and apoptosis regulator protein from homo sapiens.

3DCY: “Crystal structure a TP53-induced glycolysis and apoptosis regulator protein from homo sapiens.”. X-ray diffraction, 1 ligand (PO4), 2 pockets (best druggability 0.63). MolNFT v1 #61147 on GenesisL1: 3D structure, binding sites and…

PDB: 3DCY
Type: protein
Length: 247 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regulator protein
UniProt: Q9NQ88
Ligands: PO4
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Regulator protein	protein	247	39% helix, 20% strand	Q9NQ88

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

2 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	340	0.63	0.79	36	PO4
2	64	0.41	0.80	21	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

3DCY · Crystal Structure a TP53-induced glycolysis and apoptosis regulator protein from Homo… · the same entry in another collection · chain A against A, TM-score 1.00
Q9NQ88 · AlphaFold monomer V2.0 prediction for fructose-2,6-bisphosphatase tigar (Q9NQ88) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9NQ88
Elsewhere: RCSB PDB 3DCY · PDBe 3DCY · UniProt Q9NQ88

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