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Structure of human erythrocytic spectrin alpha chain repeats 16-17

Analyse Structure of human erythrocytic spectrin alpha chain repeats 16-17 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J4O
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spectrin alpha chain, erythrocytic 1
UniProt: P02549
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 86% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spectrin alpha chain, erythrocytic 1	protein	222	86% helix, 0% strand	P02549

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 4 copies · chains A
PG4 · Tetraethylene glycol · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.34	0.76	10	empty

Compared structures

5J4O · Structure of human erythrocytic Spectrin alpha chain repeats 16-17 · the same entry in another collection · chain A against A, TM-score 1.00
P02549 · AlphaFold monomer V2.0 prediction for spectrin alpha chain, erythrocytic 1 (P02549) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 P02549
Elsewhere: RCSB PDB 5J4O · PDBe 5J4O · UniProt P02549

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