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Crystal structure of NPR1

Analyse Crystal 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: 7MK3
Type: protein
Length: 726 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regulatory protein NPR1
UniProt: P93002
Ligands: ZN, CL
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Regulatory protein NPR1	protein	361	60% helix, 4% strand	P93002
B	Regulatory protein NPR1	protein	365	61% helix, 5% strand	P93002

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 5 copies · chains A, B
GOL · Glycerol · additive · 10 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	936	0.75	0.78	103	GOL, CL
2	852	0.75	0.79	95	GOL, CL
3	108	0.43	0.78	22	empty
4	90	0.35	0.74	15	empty
5	56	0.33	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 1340 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

7MK3 · Crystal 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 0.95

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 7MK3 · PDBe 7MK3 · UniProt P93002

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