Research workbench
Crystal structure of odorant binding protein 48 from anopheles gambiae at 3.3 ångström resolution
Analyse Crystal structure of odorant binding protein 48 from anopheles gambiae at 3.3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KYN
- Type
- protein
- Length
- 688 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Odorant binding protein-8
- UniProt
- Q8MMI9
- Pockets
- 11 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Odorant binding protein-8 | protein | 172 | 60% helix, 2% strand | Q8MMI9 |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 998 | 0.88 | 0.89 | 110 | empty |
| 2 | 849 | 0.87 | 0.89 | 100 | empty |
| 3 | 206 | 0.74 | 0.90 | 32 | empty |
| 4 | 93 | 0.66 | 0.91 | 22 | empty |
| 5 | 83 | 0.63 | 0.90 | 21 | empty |
Interfaces
6 interfaces between chains.
- B–D · 2104 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 2059 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 445 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 417 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 263 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 disulfide (disulfide).
Compared structures
- 4KYN · Crystal structure of odorant binding protein 48 from Anopheles gambiae at 3.3 Angstrom… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8MMI9
- Elsewhere: RCSB PDB 4KYN · PDBe 4KYN · UniProt Q8MMI9
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