Research workbench
Solution NMR structure of the holo form of a ribonuclease H domain from D.HAFNIENSE, northeast structural genomics consortium target DHR1A
Analyse Solution NMR structure of the holo form of a ribonuclease H domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KW4
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q24WL3
- Ligands
- MG
- Pockets
- 2 · best druggability 0.58
Structure
solution nmr · 1 distinct chain · 29% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 147 | 29% helix, 5% strand | Q24WL3 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.58 | 0.84 | 27 | empty |
| 2 | 119 | 0.46 | 0.78 | 24 | empty |
Compared structures
- 2KW4 · Solution NMR Structure of the Holo Form of a Ribonuclease H domain from D.hafniense… · 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 Q24WL3
- Elsewhere: RCSB PDB 2KW4 · PDBe 2KW4 · UniProt Q24WL3
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