Research workbench
5'-nucleotidase from E. COLI
Analyse 5'-nucleotidase from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2USH
- Type
- protein
- Length
- 1,026 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-nucleotidase
- EC
- 3.1.3.5
- UniProt
- P07024
- Ligands
- ZN, WO4
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5'-nucleotidase (EC 3.1.3.5) | protein | 506 | 30% helix, 28% strand | P07024 |
| B | 5'-nucleotidase (EC 3.1.3.5) | protein | 520 | 28% helix, 29% strand | P07024 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 954 | 0.77 | 0.79 | 103 | empty |
| 2 | 1159 | 0.76 | 0.79 | 103 | ZN |
| 3 | 120 | 0.42 | 0.77 | 21 | empty |
| 4 | 122 | 0.40 | 0.76 | 19 | empty |
| 5 | 119 | 0.39 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 523 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P07024
- Elsewhere: RCSB PDB 2USH · PDBe 2USH · UniProt P07024
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