Research workbench
Murine alloreactive scfv TCR-peptide-MHC class I molecule complex
Analyse Murine alloreactive scfv TCR-peptide-MHC class I molecule complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FO0
- Type
- protein
- Length
- 610 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (allogeneic H-2KB MHC class I molecule); Protein (beta-2 microglobulin)…
- UniProt
- P01901, P01887
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 5 distinct chains · 14% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Protein (allogeneic H-2KB MHC class I molecule) | protein | 276 | 28% helix, 38% strand | P01901 |
| L | Protein (beta-2 microglobulin) | protein | 99 | 0% helix, 49% strand | P01887 |
| P | Naturally processed octapeptide PBM1 | protein | 8 | 0% helix, 0% strand | — |
| A | Protein (BM3.3 T cell receptor alpha-chain) | protein | 115 | 5% helix, 50% strand | — |
| B | Protein (BM3.3 T cell receptor beta-chain) | protein | 112 | 0% helix, 56% strand | — |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.76 | 0.81 | 71 | empty |
| 2 | 654 | 0.66 | 0.76 | 55 | empty |
| 3 | 255 | 0.53 | 0.76 | 45 | empty |
| 4 | 130 | 0.51 | 0.80 | 29 | empty |
| 5 | 80 | 0.31 | 0.74 | 22 | empty |
Interfaces
6 interfaces between chains.
- H–L · 1178 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 975 Ų buried · 18 hydrogen bonds · protein-protein
- H–P · 901 Ų buried · 22 hydrogen bonds · protein-protein
- H–B · 414 Ų buried · 6 hydrogen bonds · protein-protein
- H–A · 317 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1FO0 · Murine alloreactive scfv TCR-peptide-MHC class I molecule complex · the same entry in another collection · chain L against L, TM-score 1.00
- P01887 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P01887) · a predicted model of the same protein · chain L against A, TM-score 0.99
- P01901 · AlphaFold monomer V2.0 prediction for H-2 class I histocompatibility antigen, K-B alpha… · a predicted model of the same protein · chain H against A, TM-score 0.96
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 P01901
- Every structure of UniProt P01887
- Elsewhere: RCSB PDB 1FO0 · PDBe 1FO0 · UniProt P01901 · UniProt P01887
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