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Structure of a rossmann-fold NAD(P)-binding family protein from shigella flexneri.
Analyse Structure of a rossmann-fold NAD(P)-binding family protein from shigella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QVO
- Type
- protein
- Length
- 197 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nmra family protein
- UniProt
- E3Y2F5
- Ligands
- MNB
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nmra family protein | protein | 197 | 31% helix, 25% strand | E3Y2F5 |
Ligands and binding sites
- MNB · 5-mercapto-2-nitro-benzoic acid · ligand · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.50 | 0.77 | 20 | empty |
| 2 | 181 | 0.50 | 0.77 | 27 | empty |
Modifications
Observed in the structure: 5 modified, 1 covalent (engineered, covalent ligand).
Compared structures
- 3QVO · Structure of a Rossmann-fold NAD(P)-binding family protein from Shigella flexneri. · 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 E3Y2F5
- Elsewhere: RCSB PDB 3QVO · PDBe 3QVO · UniProt E3Y2F5
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