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Crystal structure of the complex of lactoferrin with 6- (HYDROXYMETHYL)OXANE-2,3,4,5-tetrol at 3.49 a resolution
Analyse Crystal structure of the complex of lactoferrin with 6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CR9
- Type
- protein
- Length
- 689 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lactotransferrin
- EC
- 3.4.21.-
- UniProt
- O77811
- Ligands
- GLC, FE
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lactotransferrin (EC 3.4.21.-) | 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 | 254 | 0.76 | 0.89 | 40 | empty |
| 2 | 182 | 0.76 | 0.92 | 38 | empty |
| 3 | 587 | 0.68 | 0.77 | 63 | empty |
| 4 | 287 | 0.67 | 0.82 | 38 | empty |
| 5 | 117 | 0.44 | 0.77 | 18 | 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 3CR9 · PDBe 3CR9 · UniProt O77811
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