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Cryo-EM structure of ligand-free human SARM1

Analyse Cryo-EM structure of ligand-free human SARM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LD0
Type: protein
Length: 4,720 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD(+) hydrolase SARM1
EC: 3.2.2.6, 3.2.2.-
UniProt: Q6SZW1
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 61% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	NAD(+) hydrolase SARM1 (EC 3.2.2.6, 3.2.2.-)	protein	590	61% helix, 3% strand	Q6SZW1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	996	0.83	0.84	111	empty
2	1082	0.83	0.84	117	empty
3	858	0.82	0.84	98	empty
4	721	0.81	0.85	76	empty
5	446	0.80	0.88	59	empty

Interfaces

8 interfaces between chains.

A–B · 2401 Å² buried · 31 hydrogen bonds · protein-protein
F–G · 2395 Å² buried · 34 hydrogen bonds · protein-protein
G–H · 2386 Å² buried · 29 hydrogen bonds · protein-protein
E–F · 2382 Å² buried · 30 hydrogen bonds · protein-protein
A–H · 2375 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

7LD0 · Cryo-EM structure of ligand-free Human SARM1 · the same entry in another collection · chain A against A, 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 Q6SZW1
Elsewhere: RCSB PDB 7LD0 · PDBe 7LD0 · UniProt Q6SZW1

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