MolNFT v1 · #173072 · protein
HSARM1 NAD+ complex
7ANW · NAD(+) hydrolase SARM1: “HSARM1 NAD+ complex”. Electron microscopy, 1 ligand (NAD), 20 pockets (best druggability 0.84). MolNFT v1 #173072 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7ANW
- Type
- protein
- Length
- 5,160 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
- Ligands
- NAD
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 57% 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 | 645 | 57% helix, 3% strand | Q6SZW1 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1069 | 0.84 | 0.85 | 108 | empty |
| 2 | 768 | 0.84 | 0.87 | 120 | empty |
| 3 | 1028 | 0.83 | 0.85 | 110 | empty |
| 4 | 1032 | 0.83 | 0.84 | 106 | empty |
| 5 | 485 | 0.81 | 0.88 | 72 | empty |
Interfaces
16 interfaces between chains.
- A–H · 2452 Ų buried · 28 hydrogen bonds · protein-protein
- D–E · 2452 Ų buried · 28 hydrogen bonds · protein-protein
- B–C · 2451 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 2451 Ų buried · 28 hydrogen bonds · protein-protein
- F–G · 2450 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 7ANW · hSARM1 NAD+ complex · 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 7ANW · PDBe 7ANW · UniProt Q6SZW1
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