Research workbench
Crystal structure of xanthosine monophosphate phosphatase complex with xmp
Analyse Crystal structure of xanthosine monophosphate phosphatase complex with xmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EF7
- Type
- protein
- Length
- 236 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AT2G32150/F22D22.10
- UniProt
- Q9SKY5
- Ligands
- XMP, 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 | AT2G32150/F22D22.10 | protein | 236 | 48% helix, 11% strand | Q9SKY5 |
Ligands and binding sites
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 | 357 | 0.76 | 0.86 | 38 | MG, XMP |
| 2 | 56 | 0.33 | 0.77 | 22 | empty |
Compared structures
- 7EF7 · Crystal Structure of Xanthosine monophosphate phosphatase complex with XMP · 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 7EF7 · PDBe 7EF7 · UniProt Q9SKY5
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