MolNFT v1 · #171805 · protein
Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor
6ZH5: “Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor”. Electron microscopy, 1 ligand (FE), 20 pockets (best druggability 0.75). MolNFT v1 #171805 on GenesisL1: 3D structure…
- PDB
- 6ZH5
- Type
- protein
- Length
- 4,272 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin
- UniProt
- Q9CPX4
- Ligands
- FE
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| Z, A, C, E, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, B, D, F | Ferritin | protein | 178 | 74% helix, 1% strand | Q9CPX4 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 16 copies · chains A, G, V, C, N, F, H, R, W, I, M, T, J, P, Q, K, S, U, Z, L, D, E, O, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 895 | 0.75 | 0.79 | 87 | empty |
| 2 | 665 | 0.74 | 0.80 | 67 | empty |
| 3 | 528 | 0.73 | 0.82 | 69 | empty |
| 4 | 629 | 0.73 | 0.80 | 67 | empty |
| 5 | 681 | 0.72 | 0.79 | 73 | empty |
Interfaces
72 interfaces between chains.
- O–P · 1446 Ų buried · 26 hydrogen bonds · protein-protein
- K–L · 1446 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 1434 Ų buried · 26 hydrogen bonds · protein-protein
- Q–R · 1433 Ų buried · 27 hydrogen bonds · protein-protein
- M–N · 1428 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 6ZH5 · Folding of an iron binding peptide in response to sedimentation is resolved using… · the same entry in another collection · chain Z against Z, 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 Q9CPX4
- Elsewhere: RCSB PDB 6ZH5 · PDBe 6ZH5 · UniProt Q9CPX4
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