Research workbench
Crystal structure of a putative endoribonuclease L-psp from entamoeba histolytica, orthorhombic form
Analyse Crystal structure of a putative endoribonuclease L-psp from entamoeba… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M4S
- Type
- protein
- Length
- 751 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative endoribonuclease L-psp
- UniProt
- C4LXT9
- Ligands
- CL
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Putative endoribonuclease L-psp | protein | 125 | 31% helix, 35% strand | C4LXT9 |
| F | Putative endoribonuclease L-psp | protein | 126 | 31% helix, 35% strand | C4LXT9 |
Ligands and binding sites
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.81 | 0.99 | 31 | empty |
| 2 | 113 | 0.81 | 0.99 | 31 | empty |
| 3 | 878 | 0.72 | 0.77 | 77 | empty |
| 4 | 117 | 0.59 | 0.85 | 18 | empty |
| 5 | 108 | 0.57 | 0.85 | 20 | empty |
Interfaces
9 interfaces between chains.
- A–C · 939 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 915 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 909 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 902 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 891 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3M4S · Crystal structure of a putative endoribonuclease L-PSP from Entamoeba histolytica… · 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 C4LXT9
- Elsewhere: RCSB PDB 3M4S · PDBe 3M4S · UniProt C4LXT9
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