Research workbench
Globular domain of herpesvirus saimiri ORF57
Analyse Globular domain of herpesvirus saimiri ORF57 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HAT
- Type
- protein
- Length
- 544 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MRNA export factor ICP27 homolog
- UniProt
- P13199
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MRNA export factor ICP27 homolog | protein | 271 | 61% helix, 3% strand | P13199 |
| B | MRNA export factor ICP27 homolog | protein | 273 | 61% helix, 3% strand | P13199 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 829 | 0.73 | 0.78 | 88 | empty |
| 2 | 355 | 0.58 | 0.76 | 40 | empty |
| 3 | 75 | 0.42 | 0.80 | 18 | empty |
| 4 | 82 | 0.38 | 0.77 | 21 | empty |
| 5 | 60 | 0.38 | 0.79 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 3794 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 6HAT · Globular domain of herpesvirus saimiri ORF57 · 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 P13199
- Elsewhere: RCSB PDB 6HAT · PDBe 6HAT · UniProt P13199
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