Research workbench
Crystal structure of the human cytomegalovirus DNA polymerase subunit, UL44
Analyse Crystal structure of the human cytomegalovirus DNA polymerase subunit, UL44 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T6L
- Type
- protein
- Length
- 249 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase processivity factor
- UniProt
- P16790
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase processivity factor | protein | 249 | 19% helix, 45% strand | P16790 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.42 | 0.76 | 21 | empty |
| 2 | 61 | 0.28 | 0.74 | 18 | empty |
Compared structures
- 1T6L · Crystal Structure of the Human Cytomegalovirus DNA Polymerase Subunit, UL44 · 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 P16790
- Elsewhere: RCSB PDB 1T6L · PDBe 1T6L · UniProt P16790
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