Research workbench
Crystal structure of human transferrin bound to triferic fpc iron pyrophosphate
Analyse Crystal structure of human transferrin bound to triferic fpc iron pyrophosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CTC
- Type
- protein
- Length
- 673 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serotransferrin
- UniProt
- P02787
- Ligands
- POP, FE, CO3
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serotransferrin | protein | 673 | 37% helix, 19% strand | P02787 |
Ligands and binding sites
- POP · Pyrophosphate 2- · ligand · chains A
- FE · Fe (III) ion · metal · 2 copies · chains A
- CO3 · Carbonate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.78 | 0.98 | 23 | empty |
| 2 | 581 | 0.71 | 0.80 | 58 | empty |
| 3 | 220 | 0.64 | 0.83 | 42 | empty |
| 4 | 134 | 0.42 | 0.75 | 35 | empty |
| 5 | 57 | 0.41 | 0.81 | 18 | empty |
Modifications
Observed in the structure: 19 disulfide (disulfide).
Compared structures
- 6CTC · Crystal structure of human transferrin bound to Triferic FPC iron pyrophosphate · the same entry in another collection · chain A against A, TM-score 1.00
- P02787 · AlphaFold monomer V2.0 prediction for serotransferrin (P02787) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P02787
- Elsewhere: RCSB PDB 6CTC · PDBe 6CTC · UniProt P02787
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