MolNFT v1 · #127420 · protein

Cryoem structure of crenactin double helical filament at 3.8A resolution

5MW1 · ACTIN/ACTIN family protein: “Cryoem structure of crenactin double helical filament at 3.8A resolution”. Electron microscopy, 1 ligand (ADP), 20 pockets (best druggability 0.83). MolNFT v1 #127420 on GenesisL1: 3D structure, binding…

PDB: 5MW1
Type: protein
Length: 2,556 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ACTIN/ACTIN family protein
UniProt: A3MWN5
Ligands: ADP
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, C, D, E, F	ACTIN/ACTIN family protein	protein	426	42% helix, 18% strand	A3MWN5

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains B, A, C, D, E, F

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1040	0.83	0.84	110	empty
2	593	0.80	0.86	65	empty
3	488	0.80	0.87	71	empty
4	418	0.79	0.88	61	empty
5	807	0.78	0.82	69	empty

Interfaces

9 interfaces between chains.

B–F · 1450 Å² buried · 18 hydrogen bonds · protein-protein
A–D · 1449 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 1444 Å² buried · 18 hydrogen bonds · protein-protein
D–E · 1442 Å² buried · 18 hydrogen bonds · protein-protein
A–F · 1171 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5MW1 · cryoEM structure of crenactin double helical filament at 3.8A resolution · the same entry in another collection · chain F against F, TM-score 1.00
A3MWN5 · AlphaFold monomer V2.0 prediction for crenactin (A3MWN5) · a predicted model of the same protein · chain E against A, TM-score 0.92

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 A3MWN5
Elsewhere: RCSB PDB 5MW1 · PDBe 5MW1 · UniProt A3MWN5

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