Research workbench
Bovin alpha-lactalbumin binding with zinc ions
Analyse Bovin alpha-lactalbumin binding with zinc ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WQG
- Type
- protein
- Length
- 725 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-lactalbumin
- UniProt
- P00711
- Ligands
- ZN
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E, F | Alpha-lactalbumin | protein | 121 | 45% helix, 10% strand | P00711 |
| B | Alpha-lactalbumin | protein | 120 | 40% helix, 12% strand | P00711 |
Ligands and binding sites
- ZN · Zinc ion · metal · 7 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 600 | 0.75 | 0.82 | 55 | empty |
| 2 | 1088 | 0.73 | 0.76 | 90 | empty |
| 3 | 247 | 0.49 | 0.74 | 34 | empty |
| 4 | 132 | 0.48 | 0.78 | 20 | empty |
| 5 | 149 | 0.43 | 0.75 | 25 | empty |
Interfaces
10 interfaces between chains.
- A–B · 521 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 358 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 283 Ų buried · 5 hydrogen bonds · protein-protein
- D–E · 268 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 216 Ų buried · 5 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 7WQG · PDBe 7WQG · UniProt P00711
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