MolNFT v1 · #153030 · protein
Complex structure of gy-14 and pd-1
6J14 · Gy-14 heavy chain V fragment: “Complex structure of gy-14 and pd-1”. X-ray diffraction, 2 pockets (best druggability 0.51). MolNFT v1 #153030 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6J14
- Type
- protein
- Length
- 325 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gy-14 heavy chain V fragment; Gy-14 light chain V fragment; Programmed cell death protein…
- UniProt
- Q15116
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 3 distinct chains · 4% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gy-14 heavy chain V fragment | protein | 113 | 5% helix, 56% strand | — |
| B | Gy-14 light chain V fragment | protein | 112 | 3% helix, 47% strand | — |
| G | Programmed cell death protein 1 | protein | 100 | 3% helix, 57% strand | Q15116 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.51 | 0.75 | 38 | empty |
| 2 | 86 | 0.36 | 0.75 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 887 Ų buried · 10 hydrogen bonds · protein-protein
- A–G · 527 Ų buried · 11 hydrogen bonds · protein-protein
- B–G · 224 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 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 Q15116
- Elsewhere: RCSB PDB 6J14 · PDBe 6J14 · UniProt Q15116
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