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Anomalous substructure of alpha-lactalbumin
Analyse Anomalous substructure of alpha-lactalbumin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G4N
- Type
- protein
- Length
- 732 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-lactalbumin
- UniProt
- P00711
- Ligands
- CA, K
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Alpha-lactalbumin | protein | 122 | 42% helix, 10% strand | P00711 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, B, C, D, E, F
- K · Potassium ion · metal · 2 copies · chains A, B
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 | 388 | 0.58 | 0.75 | 47 | empty |
Interfaces
2 interfaces between chains.
- C–E · 296 Ų buried · 3 hydrogen bonds · protein-protein
- B–E · 116 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 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 P00711
- Elsewhere: RCSB PDB 2G4N · PDBe 2G4N · UniProt P00711
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