Research workbench
Structure of HI0073 from haemophilus influenzae, the nucleotide binding domain of the HI0073/HI0074 two protein nucleotidyl transferase.
Analyse Structure of HI0073 from haemophilus influenzae, the nucleotide binding domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NO5
- Type
- protein
- Length
- 202 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein HI0073
- UniProt
- P43933
- Ligands
- ZN, NA, SO4
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein HI0073 | protein | 100 | 42% helix, 20% strand | P43933 |
| B | Hypothetical protein HI0073 | protein | 102 | 38% helix, 20% strand | P43933 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B
- NA · Sodium ion · metal · chains B
- SO4 · Sulfate ion · ion · 2 copies · chains B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.47 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 399 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1NO5 · Structure of HI0073 from Haemophilus influenzae, the nucleotide binding domain of the… · the same entry in another collection · chain A against A, TM-score 1.00
- P43933 · AlphaFold monomer V2.0 prediction for probable protein adenylyltransferase mnta (P43933) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P43933
- Elsewhere: RCSB PDB 1NO5 · PDBe 1NO5 · UniProt P43933
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