Research workbench

Crystal structure of myoferlin C2A with divalent cation

Analyse Crystal structure of myoferlin C2A with divalent cation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EEL
Type: protein
Length: 387 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9NZM1
Ligands: SR

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	—	protein	129	—	Q9NZM1

Ligands and binding sites

SR · Strontium ion · metal · 6 copies · chains A, B, C

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

Compared structures

6EEL · Crystal Structure of Myoferlin C2A with divalent cation · the same entry in another collection · chain A against A, TM-score 1.00
Q9NZM1 · AlphaFold monomer V2.0 prediction for myoferlin (Q9NZM1) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q9NZM1
Elsewhere: RCSB PDB 6EEL · PDBe 6EEL · UniProt Q9NZM1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.