MolNFT v1 · #25296 · protein

Crystal structure of ferritin (TM1128) from thermotoga maritima at 2.00 a resolution

1VLG: “Crystal structure of ferritin (TM1128) from thermotoga maritima at 2.00 a resolution”. X-ray diffraction, 2 ligands (FE, SO4), 18 pockets (best druggability 0.76). MolNFT v1 #25296 on GenesisL1: 3D structure, binding sites and…

PDB: 1VLG
Type: protein
Length: 1,312 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferritin
UniProt: Q9X0L2
Ligands: FE, SO4
Pockets: 18 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Ferritin	protein	164	78% helix, 1% strand	Q9X0L2

Ligands and binding sites

FE · Fe (III) ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
SO4 · Sulfate ion · ion · 14 copies · chains A, C, B, D, E, F, H
GOL · Glycerol · additive · 9 copies · chains B, C, E, F, G, H

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

Pockets

18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	486	0.76	0.84	29	empty
2	256	0.71	0.85	28	empty
3	260	0.71	0.85	26	empty
4	261	0.70	0.84	27	empty
5	591	0.68	0.77	61	empty

Interfaces

12 interfaces between chains.

A–F · 1266 Å² buried · 33 hydrogen bonds · protein-protein
B–E · 1266 Å² buried · 27 hydrogen bonds · protein-protein
C–D · 1263 Å² buried · 27 hydrogen bonds · protein-protein
G–H · 1218 Å² buried · 27 hydrogen bonds · protein-protein
D–E · 531 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1VLG · Crystal structure of Ferritin (TM1128) from Thermotoga maritima at 2.00 A resolution · the same entry in another collection · chain A against A, 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 Q9X0L2
Elsewhere: RCSB PDB 1VLG · PDBe 1VLG · UniProt Q9X0L2

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