Research workbench

Cryoem structure of NPR1

Analyse Cryoem structure of NPR1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MK2
Type: protein
Length: 708 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regulatory protein NPR1
UniProt: P93002
Ligands: ZN
Pockets: 7 · best druggability 0.74

Structure

electron microscopy · 1 distinct chain · 58% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Regulatory protein NPR1	protein	354	58% helix, 4% strand	P93002

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	798	0.74	0.79	87	empty
2	619	0.74	0.81	64	empty
3	341	0.57	0.76	35	empty
4	78	0.51	0.84	22	empty
5	233	0.51	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 1390 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7MK2 · CryoEM Structure of NPR1 · the same entry in another collection · chain A against A, TM-score 1.00
P93002 · AlphaFold monomer V2.0 prediction for regulatory protein NPR1 (P93002) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P93002
Elsewhere: RCSB PDB 7MK2 · PDBe 7MK2 · UniProt P93002

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