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Crystal structure of thermotoga maritima ferritin mutant at 2.3 ångström resolution

Analyse Crystal structure of thermotoga maritima ferritin mutant at 2.3 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DL5
Type: protein
Length: 289 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferritin
EC: 1.16.3.2
UniProt: G4FEM0
Ligands: MG, FE
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 78% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Ferritin (EC 1.16.3.2)	protein	145	78% helix, 1% strand	G4FEM0
A	Ferritin (EC 1.16.3.2)	protein	144	78% helix, 1% strand	G4FEM0

Ligands and binding sites

MG · Magnesium ion · metal · 6 copies · chains H, A
FE · Fe (III) ion · metal · 2 copies · chains H, A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	221	0.74	0.88	33	empty

Interfaces

1 interface between chains.

H–A · 1254 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

7DL5 · Crystal structure of Thermotoga Maritima ferritin mutant at 2.3 Angstrom resolution · the same entry in another collection · chain H against H, 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 G4FEM0
Elsewhere: RCSB PDB 7DL5 · PDBe 7DL5 · UniProt G4FEM0

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