MolNFT v2 · #157505 · protein
Human apo ferritin frozen on TEM grid with amorphous carbon supporting film
6M52: “Human apo ferritin frozen on TEM grid with amorphous carbon supporting film”. Electron microscopy at 2.6, 1 ligand (FE2). MolNFT v2 #157505 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6M52
- Type
- protein
- Length
- 4,104 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Homo sapiens
- UniProt
- P02794
- Ligands
- FE2
Structure
electron microscopy · resolution 2.6 · 1 distinct chain.
| 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 | — | protein | 171 | — | P02794 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 6 copies · chains A, D, Q, T, B, C, R, S, E, H, M, P, F, G, N, O, I, L, V, W, J, K, U, X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6M52 · Human apo ferritin frozen on tem grid with amorphous carbon supporting film · the same entry in another collection · chain K against K, 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 P02794
- Elsewhere: RCSB PDB 6M52 · PDBe 6M52 · UniProt P02794
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