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Human H chain ferritin mutant-mbp

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

PDB: 6JPS
Type: protein
Length: 4,128 residues
Chains: 24
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferritin
UniProt: Q6NS36
Pockets: 20 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X	Ferritin	protein	172	72% helix, 1% strand	Q6NS36

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.75	0.98	13	empty
2	65	0.74	0.98	14	empty
3	62	0.74	0.98	14	empty
4	57	0.73	0.99	12	empty
5	58	0.73	0.98	13	empty

Interfaces

72 interfaces between chains.

J–W · 1677 Å² buried · 37 hydrogen bonds · protein-protein
I–P · 1677 Å² buried · 37 hydrogen bonds · protein-protein
C–X · 1676 Å² buried · 36 hydrogen bonds · protein-protein
D–O · 1674 Å² buried · 36 hydrogen bonds · protein-protein
L–S · 1670 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

6JPS · Human H chain ferritin mutant-MBP · the same entry in another collection · chain C against C, 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 Q6NS36
Elsewhere: RCSB PDB 6JPS · PDBe 6JPS · UniProt Q6NS36

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