Research workbench
High-resolution X-ray studies on rabbit serum transferrin: preliminary structure analysis of the N-terminal half- molecule at 2.3 ångströms resolution
Analyse High-resolution X-ray studies on rabbit serum transferrin: preliminary… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TFD
- Type
- protein
- Length
- 294 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transferrin
- UniProt
- P19134
- Ligands
- FE, CO3
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transferrin | protein | 294 | 26% helix, 19% strand | P19134 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.75 | 0.89 | 41 | empty |
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 1TFD · High-resolution X-ray studies on rabbit serum transferrin: preliminary structure analysis… · the same entry in another collection · chain A against A, TM-score 1.00
- P19134 · AlphaFold monomer V2.0 prediction for serotransferrin (P19134) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P19134
- Elsewhere: RCSB PDB 1TFD · PDBe 1TFD · UniProt P19134
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.