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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
- 6WL4
- Type
- protein
- Length
- 1,269 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-val-tyr-gln-gly-leu…
- UniProt
- P01901
- Pockets
- 18 · best druggability 0.74
Structure
x-ray diffraction · 6 distinct chains · 17% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | H-2 class I histocompatibility antigen, K-B alpha chain | protein | 178 | 38% helix, 33% strand | P01901 |
| B, E, H | Arg-gly-tyr-val-tyr-gln-gly-leu | protein | 8 | 0% helix, 0% strand | — |
| C | N15 pretcr beta | protein | 237 | 7% helix, 52% strand | — |
| D, G | H-2 class I histocompatibility antigen, K-B alpha chain | protein | 177 | 35% helix, 31% strand | P01901 |
| F | N15 pretcr beta | protein | 238 | 8% helix, 49% strand | — |
| I | N15 pretcr beta | protein | 238 | 6% helix, 48% 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 | 719 | 0.74 | 0.80 | 77 | empty |
| 2 | 123 | 0.60 | 0.85 | 20 | empty |
| 3 | 110 | 0.57 | 0.85 | 30 | empty |
| 4 | 217 | 0.50 | 0.76 | 27 | empty |
| 5 | 169 | 0.50 | 0.77 | 25 | empty |
Interfaces
16 interfaces between chains.
- A–B · 926 Ų buried · 19 hydrogen bonds · protein-protein
- D–E · 915 Ų buried · 21 hydrogen bonds · protein-protein
- G–H · 905 Ų buried · 20 hydrogen bonds · protein-protein
- D–I · 881 Ų buried · 16 hydrogen bonds · protein-protein
- F–G · 757 Ų buried · 15 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 6WL4 · PDBe 6WL4 · UniProt P01901
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