MolNFT v1 · #155557 · protein

Shrimp ferritin-T158R

6LBC: “Shrimp ferritin-T158R”. X-ray diffraction, 1 ligand (FE), 5 pockets (best druggability 0.76). MolNFT v1 #155557 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6LBC
Type: protein
Length: 1,014 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferritin
EC: 1.16.3.1
UniProt: T2B7E1
Ligands: FE
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Ferritin (EC 1.16.3.1)	protein	169	74% helix, 1% strand	T2B7E1

Ligands and binding sites

FE · Fe (III) ion · metal · 6 copies · chains A, B, C, D, E, F

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.76	0.99	14	empty
2	289	0.59	0.79	35	empty
3	263	0.57	0.78	33	empty
4	106	0.37	0.74	18	empty
5	78	0.32	0.74	14	empty

Interfaces

9 interfaces between chains.

A–B · 1465 Å² buried · 28 hydrogen bonds · protein-protein
B–E · 732 Å² buried · 9 hydrogen bonds · protein-protein
A–D · 729 Å² buried · 8 hydrogen bonds · protein-protein
D–F · 728 Å² buried · 10 hydrogen bonds · protein-protein
C–E · 728 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6LBC · shrimp ferritin-T158R · 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 T2B7E1
Elsewhere: RCSB PDB 6LBC · PDBe 6LBC · UniProt T2B7E1

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