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Human H-ferritin mutant-C90A/C102A/C130A/D144C

Analyse Human H-ferritin mutant-C90A/C102A/C130A/D144C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6J7G
Type
protein
Length
3,984 residues
Chains
24
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferritin heavy chain
EC
1.16.3.1
UniProt
P02794
Pockets
20 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, G, H, I, J, M, N, O, P, Q, R, S, T, W, X, Y, Z, a, b, e, fFerritin heavy chain (EC 1.16.3.1)protein16659% helix, 1% strandP02794

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11130.790.9817empty
21080.790.9821empty
3900.780.9915empty
4910.780.9918empty
5770.770.9916empty

Interfaces

72 interfaces between chains.

  • A–B · 1641 Ų buried · 36 hydrogen bonds · protein-protein
  • C–D · 1638 Ų buried · 24 hydrogen bonds · protein-protein
  • a–b · 1619 Ų buried · 26 hydrogen bonds · protein-protein
  • S–T · 1618 Ų buried · 24 hydrogen bonds · protein-protein
  • Q–R · 1616 Ų buried · 42 hydrogen bonds · protein-protein

Compared structures

  • 6J7G · Human H-ferritin mutant-C90A/C102A/C130A/D144C · the same entry in another collection · chain O against O, TM-score 1.00

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