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Crystal structure of postcleavge complex of escherichia COLI RNase III
Analyse Crystal structure of postcleavge complex of escherichia COLI RNase III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R97
- Type
- protein + RNA
- Length
- 508 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease 3; RNA (28-mer)
- EC
- 3.1.26.3
- UniProt
- P0A7Y0
- Ligands
- MG, K, CL
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribonuclease 3 (EC 3.1.26.3) | protein | 226 | 61% helix, 12% strand | P0A7Y0 |
| C, D | RNA (28-mer) | rna | 28 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 6 copies · chains A, C, D, B
- K · Potassium ion · metal · 2 copies · chains C, D
- CL · Chloride ion · ion · 7 copies · chains A, C, B, D
- EDO · 1,2-ethanediol · additive · 14 copies · chains A, D, B, C
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.80 | 0.93 | 48 | empty |
| 2 | 306 | 0.64 | 0.82 | 31 | MG, EDO |
| 3 | 202 | 0.59 | 0.82 | 24 | empty |
| 4 | 61 | 0.30 | 0.75 | 14 | empty |
| 5 | 56 | 0.29 | 0.75 | 14 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1178 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 916 Ų buried · 28 hydrogen bonds · protein-nucleic
- B–D · 912 Ų buried · 28 hydrogen bonds · protein-nucleic
- A–D · 744 Ų buried · 22 hydrogen bonds · protein-nucleic
- B–C · 733 Ų buried · 21 hydrogen bonds · protein-nucleic
Compared structures
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 P0A7Y0
- Elsewhere: RCSB PDB 7R97 · PDBe 7R97 · UniProt P0A7Y0
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