Research workbench
Structure of human MR1-5OH-dcf in complex with human mait a-F7 TCR
Analyse Structure of human MR1-5OH-dcf in complex with human mait a-F7 TCR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U72
- Type
- protein
- Length
- 1,600 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major histocompatibility complex class I-related gene protein; Mait T-cell receptor alpha…
- UniProt
- Q95460, P61769
- Ligands
- 7ZV
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 6 distinct chains · 14% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major histocompatibility complex class I-related gene protein | protein | 259 | 28% helix, 40% strand | Q95460 |
| B | Mait T-cell receptor alpha chain | protein | 200 | 2% helix, 45% strand | — |
| G, E | Mait T-cell receptor beta chain | protein | 243 | 7% helix, 51% strand | — |
| H, F | Beta-2-microglobulin | protein | 97 | 0% helix, 51% strand | P61769 |
| C | Major histocompatibility complex class I-related gene protein | protein | 263 | 28% helix, 42% strand | Q95460 |
| D | Mait T-cell receptor alpha chain | protein | 198 | 3% helix, 47% strand | — |
Ligands and binding sites
- 7ZV · 5-hydroxydiclofenac · ligand · chains C, D, E
- ACT · Acetate ion · additive · 3 copies · chains A, B, F
- GOL · Glycerol · additive · chains A, G
- DMS · Dimethyl sulfoxide · additive · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1155 | 0.82 | 0.83 | 99 | empty |
| 2 | 110 | 0.80 | 0.99 | 22 | 7ZV |
| 3 | 501 | 0.77 | 0.84 | 50 | empty |
| 4 | 1040 | 0.73 | 0.76 | 76 | empty |
| 5 | 1091 | 0.73 | 0.76 | 82 | empty |
Interfaces
13 interfaces between chains.
- D–E · 1980 Ų buried · 24 hydrogen bonds · protein-protein
- B–G · 1977 Ų buried · 19 hydrogen bonds · protein-protein
- C–F · 1230 Ų buried · 17 hydrogen bonds · protein-protein
- A–H · 1220 Ų buried · 17 hydrogen bonds · protein-protein
- G–C · 838 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 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 Q95460
- Every structure of UniProt P61769
- Elsewhere: RCSB PDB 5U72 · PDBe 5U72 · UniProt Q95460 · UniProt P61769
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.