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Crystal structure of the tandem SAM domains from human SARM1

Analyse Crystal structure of the tandem SAM domains from human SARM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6O0S
Type: protein
Length: 1,126 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sterile alpha and tir motif-containing protein 1
UniProt: Q6SZW1
Pockets: 12 · best druggability 0.78

Structure

x-ray diffraction · 4 distinct chains · 66% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, E, G, H	Sterile alpha and tir motif-containing protein 1	protein	140	67% helix, 0% strand	Q6SZW1
C	Sterile alpha and tir motif-containing protein 1	protein	143	64% helix, 0% strand	Q6SZW1
D	Sterile alpha and tir motif-containing protein 1	protein	139	66% helix, 0% strand	Q6SZW1
F	Sterile alpha and tir motif-containing protein 1	protein	144	66% helix, 0% strand	Q6SZW1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1072	0.78	0.80	116	empty
2	173	0.60	0.82	32	empty
3	155	0.59	0.83	26	empty
4	157	0.58	0.82	29	empty
5	145	0.57	0.83	25	empty

Interfaces

8 interfaces between chains.

F–G · 861 Å² buried · 18 hydrogen bonds · protein-protein
C–D · 844 Å² buried · 15 hydrogen bonds · protein-protein
A–H · 842 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 842 Å² buried · 20 hydrogen bonds · protein-protein
D–E · 836 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

6O0S · Crystal structure of the tandem SAM domains from human SARM1 · the same entry in another collection · chain H against H, TM-score 1.00
Q6SZW1 · AlphaFold monomer V2.0 prediction for NAD(+) hydrolase SARM1 (Q6SZW1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 6O0S · PDBe 6O0S · UniProt Q6SZW1

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