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Crystal structure of fecat-fn
Analyse Crystal structure of fecat-fn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CZU
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin light chain
- UniProt
- P02791
- Ligands
- 4LF, CD, FE, SO4
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferritin light chain | protein | 174 | 74% helix, 0% strand | P02791 |
Ligands and binding sites
- 4LF · N-[2-[2,5-bis(oxidanylidene)pyrrol-1-yl]ethyl]-2,3-bis(oxidanyl)benzamide · ligand · chains A
- CD · Cadmium ion · metal · 4 copies · chains A
- FE · Fe (III) ion · metal
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.42 | 0.77 | 17 | empty |
| 2 | 51 | 0.29 | 0.75 | 17 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
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 P02791
- Elsewhere: RCSB PDB 5CZU · PDBe 5CZU · UniProt P02791
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