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Ferritin variant with "gmg" motif

Analyse Ferritin variant with "gmg" motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JOB
Type: protein
Length: 2,064 residues
Chains: 12
Method: x-ray diffraction; solution scattering
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferritin heavy chain
EC: 1.16.3.1
UniProt: P02794
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction; solution scattering · 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	Ferritin heavy chain (EC 1.16.3.1)	protein	172	72% helix, 1% strand	P02794

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.78	0.98	19	empty
2	95	0.77	0.97	18	empty
3	87	0.76	0.97	19	empty
4	79	0.76	0.98	20	empty
5	72	0.75	0.98	13	empty

Interfaces

14 interfaces between chains.

C–D · 1598 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1569 Å² buried · 23 hydrogen bonds · protein-protein
K–L · 1551 Å² buried · 32 hydrogen bonds · protein-protein
I–J · 1521 Å² buried · 26 hydrogen bonds · protein-protein
G–H · 1510 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

6JOB · Ferritin variant with "GMG" motif · the same entry in another collection · chain L against L, 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 6JOB · PDBe 6JOB · UniProt P02794

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