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Crystal structure of human apolipoprotein a-I
Analyse Crystal structure of human apolipoprotein a-I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AV1
- Type
- protein
- Length
- 804 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apolipoprotein a-I
- UniProt
- P02647
- Pockets
- 12 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Apolipoprotein a-I | protein | 201 | 87% helix, 0% strand | P02647 |
Pockets
12 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 989 | 0.84 | 0.84 | 128 | empty |
| 2 | 866 | 0.83 | 0.84 | 119 | empty |
| 3 | 132 | 0.78 | 0.96 | 22 | empty |
| 4 | 139 | 0.78 | 0.95 | 25 | empty |
| 5 | 160 | 0.72 | 0.90 | 27 | empty |
Interfaces
6 interfaces between chains.
- A–B · 4144 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 4136 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 3362 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 3357 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 970 Ų buried · 2 hydrogen bonds · protein-protein
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 P02647
- Elsewhere: RCSB PDB 1AV1 · PDBe 1AV1 · UniProt P02647
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