Research workbench
Structure of diferric mare lactoferrin at 2.62A resolution
Analyse Structure of diferric mare lactoferrin at 2.62A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B1X
- Type
- protein
- Length
- 689 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lactoferrin
- UniProt
- O77811
- Ligands
- FE, CO3
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lactoferrin | protein | 689 | 36% helix, 19% strand | O77811 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.79 | 0.97 | 32 | empty |
| 2 | 257 | 0.76 | 0.90 | 40 | empty |
| 3 | 273 | 0.65 | 0.82 | 37 | empty |
| 4 | 406 | 0.63 | 0.77 | 46 | empty |
| 5 | 123 | 0.42 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 17 disulfide (disulfide).
Compared structures
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 O77811
- Elsewhere: RCSB PDB 1B1X · PDBe 1B1X · UniProt O77811
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