MolNFT v1 · #60125 · protein
Structure of NKG2A/CD94 bound to HLA-E
3CII · HLA class I histocompatibility antigen, alpha chain E: “Structure of NKG2A/CD94 bound to HLA-E”. X-ray diffraction, 20 pockets (best druggability 0.81). MolNFT v1 #60125 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3CII
- Type
- protein
- Length
- 1,238 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HLA class I histocompatibility antigen, alpha chain E; Beta-2-microglobulin; HLA class I…
- UniProt
- P13747, P61769, P17693, Q13241, P26715
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 5 distinct chains · 16% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | HLA class I histocompatibility antigen, alpha chain E | protein | 273 | 23% helix, 37% strand | P13747 |
| B, E | Beta-2-microglobulin | protein | 100 | 0% helix, 49% strand | P61769 |
| C, F | HLA class I histocompatibility antigen peptide | protein | 9 | 0% helix, 0% strand | P17693 |
| G, I | Natural killer cells antigen CD94 | protein | 121 | 14% helix, 30% strand | Q13241 |
| H, J | NKG2-A/NKG2-B type II integral membrane protein | protein | 116 | 15% helix, 30% strand | P26715 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 929 | 0.81 | 0.83 | 86 | empty |
| 2 | 923 | 0.79 | 0.82 | 78 | empty |
| 3 | 1097 | 0.79 | 0.81 | 93 | empty |
| 4 | 854 | 0.78 | 0.81 | 75 | empty |
| 5 | 565 | 0.76 | 0.83 | 39 | empty |
Interfaces
20 interfaces between chains.
- D–E · 1518 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1493 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 963 Ų buried · 2 hydrogen bonds · protein-protein
- D–F · 932 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 927 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 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 P13747
- Every structure of UniProt P61769
- Every structure of UniProt P17693
- Every structure of UniProt Q13241
- Every structure of UniProt P26715
- Elsewhere: RCSB PDB 3CII · PDBe 3CII · UniProt P13747 · UniProt P61769 · UniProt P17693 · UniProt Q13241 · UniProt P26715
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