Research workbench
Human cytosolic 5' nucleotidase iiib
Analyse Human cytosolic 5' nucleotidase iiib in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZEE
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- EC
- 3.1.3.91, 3.1.3.5
- UniProt
- Q969T7
- Ligands
- MG
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 7-methylguanosine phosphate-specific 5'-nucleotidase (EC 3.1.3.91, 3.1.3.5) | protein | 282 | 44% helix, 21% strand | Q969T7 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 13 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
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 | 569 | 0.69 | 0.78 | 48 | MES, MG, EDO |
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 Q969T7
- Elsewhere: RCSB PDB 7ZEE · PDBe 7ZEE · UniProt Q969T7
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