MolNFT v1 · #139287 · protein

Human ferritin mutant - E-helix deletion

5XB1 · Ferritin heavy chain: “Human ferritin mutant - E-helix deletion”. Electron microscopy, 20 pockets (best druggability 0.81). MolNFT v1 #139287 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5XB1
Type: protein
Length: 3,720 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 0.81

Structure

electron microscopy · 1 distinct chain · 71% 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	155	71% 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	146	0.81	0.97	20	empty
2	141	0.81	0.97	18	empty
3	148	0.81	0.97	20	empty
4	131	0.80	0.97	17	empty
5	130	0.79	0.97	17	empty

Interfaces

60 interfaces between chains.

E–Q · 1506 Å² buried · 25 hydrogen bonds · protein-protein
H–T · 1506 Å² buried · 25 hydrogen bonds · protein-protein
A–M · 1498 Å² buried · 25 hydrogen bonds · protein-protein
D–P · 1484 Å² buried · 24 hydrogen bonds · protein-protein
L–X · 1483 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

5XB1 · 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 5XB1 · PDBe 5XB1 · UniProt P02794

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