Research workbench
E. COLI mazf form I
Analyse E. COLI mazf form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CK9
- Type
- protein
- Length
- 210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoribonuclease mazf
- EC
- 3.1.27.-
- UniProt
- P0AE70
- Pockets
- 2 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoribonuclease mazf (EC 3.1.27.-) | protein | 106 | 20% helix, 31% strand | P0AE70 |
| B | Endoribonuclease mazf (EC 3.1.27.-) | protein | 104 | 21% helix, 32% strand | P0AE70 |
Ligands and binding sites
- 1PE · Pentaethylene glycol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.33 | 0.75 | 18 | empty |
| 2 | 96 | 0.33 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 871 Ų buried · 7 hydrogen bonds · protein-protein
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 P0AE70
- Elsewhere: RCSB PDB 5CK9 · PDBe 5CK9 · UniProt P0AE70
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