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Pretcrbeta-pmhc complex crystal structure
Analyse Pretcrbeta-pmhc complex crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WL3
- Type
- protein
- Length
- 1,267 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- H-2 class I histocompatibility antigen, K-B alpha chain; Arg-gly-tyr-leu-tyr-gln-gly-leu…
- UniProt
- P01901
- Pockets
- 18 · best druggability 0.76
Structure
x-ray diffraction · 6 distinct chains · 18% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | H-2 class I histocompatibility antigen, K-B alpha chain | protein | 179 | 41% helix, 31% strand | P01901 |
| B, E, H | Arg-gly-tyr-leu-tyr-gln-gly-leu | protein | 8 | 0% helix, 0% strand | — |
| C | N15 pretcr beta | protein | 237 | 8% helix, 50% strand | — |
| D, G | H-2 class I histocompatibility antigen, K-B alpha chain | protein | 177 | 40% helix, 31% strand | P01901 |
| F | N15 pretcr beta | protein | 238 | 7% helix, 52% strand | — |
| I | N15 pretcr beta | protein | 235 | 8% helix, 51% strand | — |
Pockets
18 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 753 | 0.76 | 0.81 | 74 | empty |
| 2 | 255 | 0.65 | 0.83 | 40 | empty |
| 3 | 185 | 0.55 | 0.80 | 29 | empty |
| 4 | 210 | 0.52 | 0.77 | 31 | empty |
| 5 | 123 | 0.47 | 0.79 | 25 | empty |
Interfaces
16 interfaces between chains.
- G–H · 918 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 896 Ų buried · 20 hydrogen bonds · protein-protein
- D–E · 894 Ų buried · 17 hydrogen bonds · protein-protein
- D–I · 783 Ų buried · 19 hydrogen bonds · protein-protein
- F–G · 676 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 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 P01901
- Elsewhere: RCSB PDB 6WL3 · PDBe 6WL3 · UniProt P01901
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