5A37: Human alpha-actinin-2

Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Determined by X-ray diffraction at 1.88 Å resolution. Released 22 Jun 2016.

Method: X-ray diffraction
Resolution: 1.88 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,854
Mol. weight: 57.26 kDa
Released: 22 Jun 2016

Explore 5A37 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5A37 contains 33 α-helices and 4 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 16 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	36-52	17
α-helix	53-55	3
α-helix	70-80	11
α-helix	83-87	5
α-helix	93-110	18
α-helix	119-123	5
α-helix	127-138	12
α-helix	139-143	5
β-strand	147-148	2	1
β-strand	151-152	2	1
α-helix	153-164	12
α-helix	178-180	3
α-helix	184-193	10
α-helix	195-197	3
α-helix	200-202	3
α-helix	208-223	16
α-helix	231-236	6
α-helix	242-256	15

Chain B: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	36-52	17
α-helix	53-55	3
α-helix	62-65	4
α-helix	70-80	11
α-helix	83-88	6
α-helix	93-110	18
α-helix	119-123	5
α-helix	127-138	12
α-helix	139-143	5
β-strand	147-148	2	2
β-strand	151-152	2	2
α-helix	153-165	13
α-helix	178-180	3
α-helix	184-193	10
α-helix	195-197	3
α-helix	200-202	3
α-helix	208-223	16
α-helix	231-235	5
α-helix	242-255	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Human alpha-actinin-2	A, B	protein	250	HOMO SAPIENS	P35609 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5A37_1 HUMAN ALPHA-ACTININ-2 (chains A, B)
GPYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLL
EVISGERLPKPDRGKMRFHKIANVNKALDYIASKVVKLVSIGAEEIVDGNVKMTLGMIWT
IILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPD
LIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAF
AGAEQAETAA

Primary citation

Hypertrophic Cardiomyopathy Mutations in the Calponin-Homology Domain of Actn2 Affect Actin Binding and Cardiomyocyte Z-Disc Incorporation. Haywood, N., Wolny, M., Rogers, B. et al. Biochem J (2016) 473:2485. DOI 10.1042/BCJ20160421 · PubMed

Other PDB entries of the same protein (UniProt P35609 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6SWT 1.2 Å, Affimer9 co-crystalised with the CH domains of alpha actinin 2.
6TS3 1.28 Å, EF-hands 3 and 4 of alpha-actinin in complex with CaMKII regulatory segment
7B56 1.45 Å, Crystal structure of CaMKII-actinin complex bound to AMPPNP
7B55 1.6 Å, Crystal structure of CaMKII-actinin complex bound to MES
5A38 1.9 Å, Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and…
7B57 1.95 Å, Crystal structure of CaMKII-actinin complex bound to ADP
5A36 2.0 Å, Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and…
5A4B 2.01 Å, Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and…
1QUU 2.5 Å, Crystal structure of two central spectrin-like repeats from alpha-actinin
7A8T 2.69 Å, Crystal structure of sarcomeric protein FATZ-1 (mini-FATZ-1 construct) in complex with…
1HCI 2.8 Å, Crystal structure of the rod domain of alpha-actinin
7ANK 3.2 Å, Crystal structure of sarcomeric protein FATZ-1 (d91-FATZ-1 construct) in complex with…

Browse structure collections

About this viewer

MolViewer shows 5A37 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.