MolNFT v1 · #148078 · protein
Crystal structure of HLA-A2 in complex with LILRB1
6EWA · HLA class I histocompatibility antigen, a-2 alpha chain: “Crystal structure of HLA-A2 in complex with LILRB1”. X-ray diffraction, 14 pockets (best druggability 0.77). MolNFT v1 #148078 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6EWA
- Type
- protein
- Length
- 1,123 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HLA class I histocompatibility antigen, a-2 alpha chain; Beta-2-microglobulin…
- UniProt
- P01892, P61769, Q9WGX1, D9IDM8
- Pockets
- 14 · best druggability 0.77
Structure
x-ray diffraction · 6 distinct chains · 16% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HLA class I histocompatibility antigen, a-2 alpha chain | protein | 276 | 26% helix, 39% strand | P01892 |
| B, F | Beta-2-microglobulin | protein | 99 | 0% helix, 52% strand | P61769 |
| C, G | Polyprotein | protein | 9 | 0% helix, 0% strand | Q9WGX1 |
| D | Lir-1 | protein | 169 | 4% helix, 44% strand | D9IDM8 |
| E | HLA class I histocompatibility antigen, a-2 alpha chain | protein | 274 | 27% helix, 40% strand | P01892 |
| H | Lir-1 | protein | 188 | 6% helix, 45% strand | D9IDM8 |
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.77 | 0.79 | 76 | empty |
| 2 | 980 | 0.77 | 0.79 | 81 | empty |
| 3 | 532 | 0.66 | 0.77 | 54 | empty |
| 4 | 508 | 0.65 | 0.77 | 50 | empty |
| 5 | 84 | 0.47 | 0.81 | 17 | empty |
Interfaces
8 interfaces between chains.
- E–F · 1388 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1375 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 861 Ų buried · 12 hydrogen bonds · protein-protein
- E–G · 833 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 643 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 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 P01892
- Every structure of UniProt P61769
- Every structure of UniProt Q9WGX1
- Every structure of UniProt D9IDM8
- Elsewhere: RCSB PDB 6EWA · PDBe 6EWA · UniProt P01892 · UniProt P61769 · UniProt Q9WGX1 · UniProt D9IDM8
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