Research workbench
Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin
Analyse Crystal structure of K206E/K296E mutant of the N-terminal half molecule of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O7U
- Type
- protein
- Length
- 2,961 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serotransferrin
- UniProt
- P02787
- Ligands
- FE, CO3
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D, E, F, G, H, I | Serotransferrin | protein | 329 | 34% helix, 22% strand | P02787 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 9 copies · chains B, A, C, D, E, F, G, H, I
- CO3 · Carbonate ion · ion · 9 copies · chains B, A, C, D, E, F, G, H, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 937 | 0.83 | 0.85 | 102 | empty |
| 2 | 1088 | 0.82 | 0.83 | 142 | empty |
| 3 | 495 | 0.81 | 0.88 | 87 | empty |
| 4 | 710 | 0.79 | 0.83 | 94 | empty |
| 5 | 407 | 0.76 | 0.86 | 57 | empty |
Interfaces
16 interfaces between chains.
- C–H · 931 Ų buried · 10 hydrogen bonds · protein-protein
- A–I · 924 Ų buried · 10 hydrogen bonds · protein-protein
- C–F · 734 Ų buried · 4 hydrogen bonds · protein-protein
- A–E · 732 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 712 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 72 disulfide (disulfide).
Compared structures
- 2O7U · Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human… · the same entry in another collection · chain I against I, TM-score 1.00
- P02787 · AlphaFold monomer V2.0 prediction for serotransferrin (P02787) · a predicted model of the same protein · chain B 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 P02787
- Elsewhere: RCSB PDB 2O7U · PDBe 2O7U · UniProt P02787
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.