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Ef-hands 3 and 4 of alpha-actinin in complex with camkii regulatory segment

Analyse Ef-hands 3 and 4 of alpha-actinin in complex with camkii regulatory segment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TS3
Type
protein
Length
180 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-actinin-2; ACE-asn-ala-arg-arg-lys-leu-lys-gly-ala-ile-leu-thr-thr…
UniProt
P35609
Ligands
ACE

Structure

x-ray diffraction · 4 distinct chains · 62% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-actinin-2protein7358% helix, 4% strandP35609
BAlpha-actinin-2protein7060% helix, 4% strandP35609
CACE-asn-ala-arg-arg-lys-leu-lys-gly-ala-ile-leu-thr-thr- met-leu-ala-thr-arg-asn-pheprotein2075% helix, 0% strand—
DACE-asn-ala-arg-arg-lys-leu-lys-gly-ala-ile-leu-thr-thr- met-leu-ala-thr-arg-asn-pheprotein1776% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 2 copies · chains C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

6 interfaces between chains.

  • A–C · 710 Ų buried · 6 hydrogen bonds · protein-protein
  • B–D · 577 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 257 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 235 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 197 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 6TS3 · EF-hands 3 and 4 of alpha-actinin in complex with CaMKII regulatory segment · 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 0.89

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