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Phascolosoma esculenta ferritin

Analyse Phascolosoma esculenta ferritin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LPE
Type: protein
Length: 688 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.99
Source: Phascolosoma esculenta
Molecule: Ferritin
EC: 1.16.3.1
UniProt: B3TFG2
Ligands: MG, SO4
Pockets: 6 · best druggability 0.74

Structure

x-ray diffraction · resolution 1.99 · 1 distinct chain · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Ferritin (EC 1.16.3.1)	protein	172	72% helix, 0% strand	B3TFG2

Ligands and binding sites

MG · Magnesium ion · metal · 12 copies · chains A, B, C, D
SO4 · Sulfate ion · ion · 15 copies · chains A, B, C, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.74	0.99	14	empty
2	71	0.43	0.81	13	empty
3	66	0.41	0.81	13	empty
4	130	0.40	0.74	23	empty
5	59	0.39	0.80	13	empty

Interfaces

2 interfaces between chains.

C–D · 1537 Å² buried · 23 hydrogen bonds · protein-protein
B–C · 70 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6LPE · Phascolosoma esculenta ferritin · 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 B3TFG2
Elsewhere: RCSB PDB 6LPE · PDBe 6LPE · UniProt B3TFG2

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