Research workbench
Uvc treated human apoferritin
Analyse Uvc treated human apoferritin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PF1
- Type
- protein
- Length
- 4,176 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02794
- Ligands
- MG, CL
Structure
electron microscopy · 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 | 174 | — | P02794 |
Ligands and binding sites
- MG · Magnesium ion · metal · 167 copies · chains A, T, O, B, L, N, C, M, R, D, E, Q, I, F, K, H, G, W, S, P, U, J, X, V
- CL · Chloride ion · ion · 96 copies · chains A, Q, W, J, B, K, V, R, C, F, U, I, D, L, M, E, H, S, G, P, X, N, T, O
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PF1 · UVC treated Human apoferritin · 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 7PF1 · PDBe 7PF1 · UniProt P02794
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