Research workbench
Structure of human transferrin receptor-transferrin complex
Analyse Structure of human transferrin receptor-transferrin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SUV
- Type
- protein
- Length
- 2,626 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transferrin receptor protein 1; Serotransferrin, N-lobe; Serotransferrin, C-lobe
- UniProt
- P02786, P02787
- Ligands
- FE, CO3
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 3 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transferrin receptor protein 1 | protein | 639 | 36% helix, 15% strand | P02786 |
| C, D | Serotransferrin, N-lobe | protein | 329 | 36% helix, 22% strand | P02787 |
| E, F | Serotransferrin, C-lobe | protein | 345 | 35% helix, 18% strand | — |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains C, D, E, F
- CO3 · Carbonate ion · ion · 4 copies · chains C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 813 | 0.84 | 0.86 | 95 | empty |
| 2 | 712 | 0.82 | 0.86 | 81 | empty |
| 3 | 220 | 0.82 | 0.95 | 56 | empty |
| 4 | 623 | 0.79 | 0.85 | 56 | empty |
| 5 | 620 | 0.78 | 0.84 | 61 | empty |
Interfaces
10 interfaces between chains.
- A–B · 3039 Ų buried · 14 hydrogen bonds · protein-protein
- A–E · 807 Ų buried · 24 hydrogen bonds · protein-protein
- B–F · 783 Ų buried · 24 hydrogen bonds · protein-protein
- D–F · 713 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 710 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 42 disulfide (disulfide).
Compared structures
- 1SUV · Structure of Human Transferrin Receptor-Transferrin Complex · the same entry in another collection · chain F against F, TM-score 1.00
- P02787 · AlphaFold monomer V2.0 prediction for serotransferrin (P02787) · a predicted model of the same protein · chain C against A, TM-score 0.98
- P02786 · AlphaFold monomer V2.0 prediction for transferrin receptor protein 1 (P02786) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P02786
- Every structure of UniProt P02787
- Elsewhere: RCSB PDB 1SUV · PDBe 1SUV · UniProt P02786 · UniProt P02787
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