MolNFT v1 · #11555 · protein
Hcmv protease dimer-interface mutant, S225Y complexed to inhibitor bilc 408
1JQ7 · Assemblin: “Hcmv protease dimer-interface mutant, S225Y complexed to inhibitor bilc 408”. X-ray diffraction, 1 ligand (0FP), 5 pockets (best druggability 0.46). MolNFT v1 #11555 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1JQ7
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Assemblin
- EC
- 3.4.21.97
- UniProt
- P16753
- Ligands
- 0FP
- Pockets
- 5 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Assemblin (EC 3.4.21.97) | protein | 210 | 29% helix, 18% strand | P16753 |
| B | Assemblin (EC 3.4.21.97) | protein | 217 | 34% helix, 21% strand | P16753 |
Ligands and binding sites
- 0FP · N-(6-aminohexanoyl)-3-methyl-L-valyl-3-methyl-L-valyl-N~1~-[(2S,3S)-3-hydroxy-4-oxo-4-{[(1R)-1-phenylpropyl]amino}butan-2-yl]-N~4~,N~4~-dimethyl-L-aspartamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 181 | 0.46 | 0.75 | 30 | empty |
| 2 | 53 | 0.39 | 0.81 | 15 | empty |
| 3 | 66 | 0.39 | 0.79 | 19 | empty |
| 4 | 70 | 0.37 | 0.78 | 15 | empty |
| 5 | 63 | 0.28 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1634 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 1JQ7 · HCMV protease dimer-interface mutant, S225Y complexed to Inhibitor BILC 408 · the same entry in another collection · chain A against A, TM-score 1.00
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 P16753
- Elsewhere: RCSB PDB 1JQ7 · PDBe 1JQ7 · UniProt P16753
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