Research workbench
Co-crystal structure of E.COLI RNase hi active site mutant (D134A*) with MN2+
Analyse Co-crystal structure of E.COLI RNase hi active site mutant (D134A*) with MN2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WSF
- Type
- protein
- Length
- 620 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease hi
- EC
- 3.1.26.4
- UniProt
- P0A7Y4
- Ligands
- MN
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Ribonuclease hi (EC 3.1.26.4) | protein | 155 | 36% helix, 31% strand | P0A7Y4 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.66 | 0.77 | 51 | empty |
Interfaces
1 interface between chains.
- A–C · 721 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1WSF · Co-crystal structure of E.coli RNase HI active site mutant (D134A*) with Mn2+ · the same entry in another collection · chain A against A, TM-score 1.00
- P0A7Y4 · AlphaFold monomer V2.0 prediction for ribonuclease hi (P0A7Y4) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P0A7Y4
- Elsewhere: RCSB PDB 1WSF · PDBe 1WSF · UniProt P0A7Y4
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