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Crystal structure of the catalytic site mutant (H157A) of the human cytomegalovirus protease
Analyse Crystal structure of the catalytic site mutant (H157A) of the human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IEC
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein P40: assemblin protease
- EC
- 3.4.21.97
- UniProt
- P16753
- Pockets
- 5 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein P40: assemblin protease (EC 3.4.21.97) | protein | 207 | 36% helix, 25% strand | P16753 |
| B | Capsid protein P40: assemblin protease (EC 3.4.21.97) | protein | 219 | 38% helix, 22% strand | P16753 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.51 | 0.87 | 15 | empty |
| 2 | 106 | 0.50 | 0.81 | 28 | empty |
| 3 | 55 | 0.38 | 0.80 | 15 | empty |
| 4 | 96 | 0.37 | 0.76 | 19 | empty |
| 5 | 69 | 0.29 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1582 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 1IEC · Crystal structure of the catalytic site mutant (H157A) of the human cytomegalovirus… · 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 1IEC · PDBe 1IEC · UniProt P16753
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