Research workbench
Crystal structure of xanthosine monophosphate phosphatase in the unliganded state
Analyse Crystal structure of xanthosine monophosphate phosphatase in the unliganded… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EF6
- Type
- protein
- Length
- 233 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xanthosine monophosphate phosphatase
- UniProt
- Q9SKY5
- Ligands
- MG
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xanthosine monophosphate phosphatase | protein | 233 | 48% helix, 11% strand | Q9SKY5 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 421 | 0.76 | 0.85 | 35 | MG |
| 2 | 71 | 0.34 | 0.76 | 24 | empty |
Compared structures
- 7EF6 · Crystal Structure of Xanthosine monophosphate phosphatase in the unliganded state · 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 Q9SKY5
- Elsewhere: RCSB PDB 7EF6 · PDBe 7EF6 · UniProt Q9SKY5
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