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Local refinement of protein 4.2, class 1 of erythrocyte ankyrin-1 complex

Analyse Local refinement of protein 4.2, class 1 of erythrocyte ankyrin-1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V0Q
Type: protein
Length: 658 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein 4.2
UniProt: P16452
Pockets: 7 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 18% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Protein 4.2	protein	658	18% helix, 41% strand	P16452

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	622	0.78	0.84	66	empty
2	282	0.70	0.84	42	empty
3	106	0.52	0.82	17	empty
4	250	0.51	0.75	27	empty
5	53	0.50	0.87	20	empty

Compared structures

7V0Q · Local refinement of protein 4.2, class 1 of erythrocyte ankyrin-1 complex · the same entry in another collection · chain X against X, TM-score 1.00
P16452 · AlphaFold monomer V2.0 prediction for protein 4.2 (P16452) · a predicted model of the same protein · chain X against A, TM-score 0.98

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 P16452
Elsewhere: RCSB PDB 7V0Q · PDBe 7V0Q · UniProt P16452

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