Research workbench

DNA-binding regulatory protein

Analyse DNA-binding regulatory protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DBQ
Type: protein
Length: 552 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Purine repressor
UniProt: P0ACP7
Ligands: MG
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Purine repressor	protein	276	41% helix, 19% strand	P0ACP7

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	872	0.76	0.80	73	MG
2	174	0.53	0.79	28	empty
3	206	0.50	0.76	27	empty
4	65	0.44	0.82	13	empty
5	103	0.37	0.74	23	empty

Interfaces

1 interface between chains.

A–B · 1660 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

1DBQ · DNA-binding regulatory protein · the same entry in another collection · chain A against A, TM-score 1.00
P0ACP7 · AlphaFold monomer V2.0 prediction for hth-type transcriptional repressor purr (P0ACP7) · a predicted model of the same protein · chain A against A, TM-score 0.86

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 P0ACP7
Elsewhere: RCSB PDB 1DBQ · PDBe 1DBQ · UniProt P0ACP7

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