Research workbench
Crystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM reconstruction of canine parvovirus and feline transferrin receptor complex
Analyse Crystal structure of the ectodomain of human transferrin receptor fitted into a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NSU
- Type
- protein
- Length
- 1,278 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transferrin receptor protein 1
- UniProt
- P02786
- Pockets
- 15 · best druggability 0.81
Structure
electron microscopy · 1 distinct chain · 36% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transferrin receptor protein 1 | protein | 639 | 36% helix, 15% strand | P02786 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 512 | 0.81 | 0.88 | 84 | empty |
| 2 | 267 | 0.80 | 0.92 | 31 | empty |
| 3 | 884 | 0.80 | 0.83 | 101 | empty |
| 4 | 261 | 0.79 | 0.91 | 30 | empty |
| 5 | 598 | 0.78 | 0.84 | 55 | empty |
Interfaces
1 interface between chains.
- A–B · 3039 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2NSU · Crystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM… · the same entry in another collection · chain A against A, TM-score 1.00
- 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
- Elsewhere: RCSB PDB 2NSU · PDBe 2NSU · UniProt P02786
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