MolNFT v1 · #176238 · protein

Cryo-EM structure of plant nlr RPP1 tetramer core part

7DFV · NAD+ hydrolase (nadase): “Cryo-EM structure of plant nlr RPP1 tetramer core part”. Electron microscopy, 20 pockets (best druggability 0.87). MolNFT v1 #176238 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7DFV
Type: protein
Length: 2,072 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD+ hydrolase (nadase)
UniProt: Q9ZSN5
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 2 distinct chains · 49% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, D	NAD+ hydrolase (nadase)	protein	520	49% helix, 11% strand	Q9ZSN5
C, A	NAD+ hydrolase (nadase)	protein	516	49% helix, 11% strand	Q9ZSN5

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	978	0.87	0.89	99	empty
2	968	0.87	0.88	89	empty
3	997	0.86	0.87	103	empty
4	766	0.84	0.87	75	empty
5	378	0.76	0.86	42	empty

Interfaces

4 interfaces between chains.

D–A · 2595 Å² buried · 27 hydrogen bonds · protein-protein
B–C · 2591 Å² buried · 27 hydrogen bonds · protein-protein
C–D · 2153 Å² buried · 20 hydrogen bonds · protein-protein
B–A · 2142 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

7DFV · Cryo-EM structure of plant NLR RPP1 tetramer core part · the same entry in another collection · chain B against B, TM-score 1.00

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 Q9ZSN5
Elsewhere: RCSB PDB 7DFV · PDBe 7DFV · UniProt Q9ZSN5

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