Research workbench
Crystal structure of the catalytic domain of FLJ14393
Analyse Crystal structure of the catalytic domain of FLJ14393 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XDV
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myc-induced nuclear antigen
- UniProt
- Q8IUF8
- Ligands
- OGA, NI, CD, MN
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myc-induced nuclear antigen | protein | 374 | 34% helix, 23% strand | Q8IUF8 |
Ligands and binding sites
- OGA · N-oxalylglycine · ligand · chains A
- NI · Nickel (II) ion · metal · 6 copies · chains A
- CD · Cadmium ion · metal · 3 copies · chains A
- MN · Manganese (II) ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · 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 | 574 | 0.67 | 0.77 | 73 | OGA, NI |
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 Q8IUF8
- Elsewhere: RCSB PDB 2XDV · PDBe 2XDV · UniProt Q8IUF8
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