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Human ferritin mutant - E-helix deletion

Analyse Human ferritin mutant - E-helix deletion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YI5
Type: protein
Length: 4,128 residues
Chains: 24
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferritin heavy chain
EC: 1.16.3.1
UniProt: P02794
Pockets: 20 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 72% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X	Ferritin heavy chain (EC 1.16.3.1)	protein	172	72% helix, 1% strand	P02794

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.73	0.97	13	empty
2	57	0.72	0.98	13	empty
3	57	0.72	0.98	12	empty
4	61	0.71	0.97	13	empty
5	61	0.71	0.97	13	empty

Interfaces

72 interfaces between chains.

K–W · 1527 Å² buried · 18 hydrogen bonds · protein-protein
B–N · 1500 Å² buried · 18 hydrogen bonds · protein-protein
A–M · 1495 Å² buried · 18 hydrogen bonds · protein-protein
G–S · 1493 Å² buried · 18 hydrogen bonds · protein-protein
J–V · 1492 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

5YI5 · human ferritin mutant - E-helix deletion · the same entry in another collection · chain K against K, TM-score 1.00

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 P02794
Elsewhere: RCSB PDB 5YI5 · PDBe 5YI5 · UniProt P02794

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