MolNFT v1 · #156789 · protein
HLA-DQ2-glia-ALPHA1
6MFG · HLA class II histocompatibility antigen, dq alpha 1 chain: “HLA-DQ2-glia-ALPHA1”. X-ray diffraction, 1 ligand (NAG), 10 pockets (best druggability 0.69). MolNFT v1 #156789 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6MFG
- Type
- protein
- Length
- 744 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HLA class II histocompatibility antigen, dq alpha 1 chain; MHC class II HLA-dq-beta-1…
- UniProt
- P01909, O19712
- Ligands
- NAG
- Pockets
- 10 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, A | HLA class II histocompatibility antigen, dq alpha 1 chain | protein | 181 | 14% helix, 44% strand | P01909 |
| E, F | MHC class II HLA-dq-beta-1 - DQ2-glia-ALPHA1 chimeric protein | protein | 191 | 20% helix, 43% strand | O19712 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1020 | 0.69 | 0.74 | 103 | empty |
| 2 | 540 | 0.61 | 0.74 | 62 | empty |
| 3 | 211 | 0.46 | 0.74 | 30 | empty |
| 4 | 149 | 0.44 | 0.75 | 21 | empty |
| 5 | 141 | 0.41 | 0.74 | 24 | empty |
Interfaces
6 interfaces between chains.
- A–F · 2650 Ų buried · 53 hydrogen bonds · protein-protein
- C–E · 2640 Ų buried · 50 hydrogen bonds · protein-protein
- E–F · 2009 Ų buried · 20 hydrogen bonds · protein-protein
- E–A · 568 Ų buried · 6 hydrogen bonds · protein-protein
- C–F · 506 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).
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 P01909
- Every structure of UniProt O19712
- Elsewhere: RCSB PDB 6MFG · PDBe 6MFG · UniProt P01909 · UniProt O19712
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