MolNFT v1 · #113029 · protein

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

5A36 · Alpha-actinin-2: “Mutations in the calponin homology domain of alpha-actinin- 2 affect actin binding and incorporation in…”. X-ray diffraction, 2 pockets (best druggability 0.68). MolNFT v1 #113029 on GenesisL1: 3D structure…

PDB: 5A36
Type: protein
Length: 463 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-actinin-2
UniProt: P35609
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-actinin-2	protein	239	62% helix, 2% strand	P35609
B	Alpha-actinin-2	protein	224	62% 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	689	0.68	0.76	57	empty
2	93	0.36	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 243 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5A36 · 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 5A36 · PDBe 5A36 · UniProt P35609

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