Research workbench
Crystal structure of a NIMC/NIMA family protein (CA_C2569) from clostridium acetobutylicum at 1.80 a resolution
Analyse Crystal structure of a NIMC/NIMA family protein (CA_C2569) from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IG6
- Type
- protein
- Length
- 282 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NIMC/NIMA family protein
- UniProt
- Q97G05
- Ligands
- FMN, UNL, SO4
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NIMC/NIMA family protein | protein | 143 | 31% helix, 41% strand | Q97G05 |
| B | NIMC/NIMA family protein | protein | 139 | 31% helix, 45% strand | Q97G05 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A, B
- UNL · Unknown ligand · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.52 | 0.75 | 28 | SO4 |
| 2 | 203 | 0.49 | 0.75 | 26 | FMN, UNL |
| 3 | 53 | 0.30 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1068 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2IG6 · Crystal structure of a nimc/nima family protein (ca_c2569) from clostridium… · 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 Q97G05
- Elsewhere: RCSB PDB 2IG6 · PDBe 2IG6 · UniProt Q97G05
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