MolNFT v1 · #113030 · protein

Mutations in the calponin homology domain of alpha-actinin-2 affect actin binding and incorporation in muscle.

5A37 · Human alpha-actinin-2: “Mutations in the calponin homology domain of alpha-actinin-2 affect actin binding and incorporation in muscle.”. X-ray diffraction, 2 pockets (best druggability 0.62). MolNFT v1 #113030 on GenesisL1: 3D…

PDB: 5A37
Type: protein
Length: 439 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human alpha-actinin-2
UniProt: P35609
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 64% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human alpha-actinin-2	protein	220	63% helix, 2% strand	P35609
B	Human alpha-actinin-2	protein	219	65% helix, 2% strand	P35609

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	459	0.62	0.76	51	empty
2	111	0.41	0.76	18	empty

Interfaces

1 interface between chains.

A–B · 281 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5A37 · Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and… · the same entry in another collection · chain A against A, TM-score 1.00
P35609 · AlphaFold monomer V2.0 prediction for alpha-actinin-2 (P35609) · a predicted model of the same protein · chain B 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 P35609
Elsewhere: RCSB PDB 5A37 · PDBe 5A37 · UniProt P35609

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