Research workbench
Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor
Analyse Folding of an iron binding peptide in response to sedimentation is resolved… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZLG
- Type
- protein
- Length
- 4,072 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin
- UniProt
- Q9CPX4
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 2 distinct chains · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F, I, N, O, T, U, Z | Ferritin | protein | 169 | 74% helix, 1% strand | Q9CPX4 |
| B, C, D, E, J, K, L, M, P, Q, R, S, V, W, X, Y | Ferritin | protein | 170 | 74% helix, 1% strand | Q9CPX4 |
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 | 169 | 0.79 | 0.94 | 20 | empty |
| 2 | 200 | 0.78 | 0.92 | 24 | empty |
| 3 | 184 | 0.77 | 0.93 | 23 | empty |
| 4 | 187 | 0.77 | 0.92 | 22 | empty |
| 5 | 196 | 0.77 | 0.92 | 23 | empty |
Interfaces
72 interfaces between chains.
- A–B · 1521 Ų buried · 16 hydrogen bonds · protein-protein
- O–P · 1506 Ų buried · 14 hydrogen bonds · protein-protein
- I–J · 1500 Ų buried · 13 hydrogen bonds · protein-protein
- U–V · 1496 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 1435 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6ZLG · Folding of an iron binding peptide in response to sedimentation is resolved using… · the same entry in another collection · chain D against D, 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 6ZLG · PDBe 6ZLG · UniProt Q9CPX4
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