Research workbench
Crystal structure of the human cytomegalovirus nuclear egress complex (nec)
Analyse Crystal structure of the human cytomegalovirus nuclear egress complex (nec) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DOB
- Type
- protein
- Length
- 402 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Virion egress protein UL31 homolog; Virion egress protein UL34 homolog
- UniProt
- P16794, P16791
- Ligands
- ZN, CA
- Pockets
- 6 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Virion egress protein UL31 homolog | protein | 237 | 40% helix, 22% strand | P16794 |
| B | Virion egress protein UL34 homolog | protein | 165 | 32% helix, 30% strand | P16791 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.49 | 0.78 | 19 | empty |
| 2 | 96 | 0.39 | 0.76 | 22 | empty |
| 3 | 81 | 0.33 | 0.75 | 18 | empty |
| 4 | 52 | 0.32 | 0.77 | 14 | empty |
| 5 | 54 | 0.32 | 0.76 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 2044 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 5DOB · Crystal structure of the Human Cytomegalovirus Nuclear Egress Complex (NEC) · 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 P16794
- Every structure of UniProt P16791
- Elsewhere: RCSB PDB 5DOB · PDBe 5DOB · UniProt P16794 · UniProt P16791
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