Research workbench
Class II MHC I-ad in complex with an influenza hemagglutinin peptide 126-138
Analyse Class II MHC I-ad in complex with an influenza hemagglutinin peptide 126-138 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IAD
- Type
- protein
- Length
- 388 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MHC class II I-ad
- UniProt
- P04228, P01921
- Pockets
- 4 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MHC class II I-ad | protein | 187 | 11% helix, 43% strand | P04228 |
| B | MHC class II I-ad | protein | 201 | 20% helix, 38% strand | P01921 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.38 | 0.74 | 19 | empty |
| 2 | 89 | 0.37 | 0.76 | 18 | empty |
| 3 | 89 | 0.33 | 0.74 | 20 | empty |
| 4 | 61 | 0.29 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2942 Ų buried · 53 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2IAD · Class II MHC I-ad in complex with an influenza hemagglutinin peptide 126-138 · the same entry in another collection · chain A against A, TM-score 1.00
- P04228 · AlphaFold monomer V2.0 prediction for H-2 class II histocompatibility antigen, a-D alpha… · a predicted model of the same protein · chain A against A, TM-score 0.93
- P01921 · AlphaFold monomer V2.0 prediction for H-2 class II histocompatibility antigen, a-D beta… · a predicted model of the same protein · chain B against A, TM-score 0.78
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 P04228
- Every structure of UniProt P01921
- Elsewhere: RCSB PDB 2IAD · PDBe 2IAD · UniProt P04228 · UniProt P01921
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