MolNFT v1 · #40105 · protein
Crystal structure of a putative 4-methylmuconolactone methylisomerase (YP_295714.1) from ralstonia eutropha JMP134 at 2.00 a resolution
2IFX · Hypothetical protein: “Crystal structure of a putative 4-methylmuconolactone methylisomerase (YP_295714.1) from ralstonia eutropha…”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.59). MolNFT v1 #40105 on…
- PDB
- 2IFX
- Type
- protein
- Length
- 203 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- Q471R3
- Ligands
- CL
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 106 | 36% helix, 27% strand | Q471R3 |
| B | Hypothetical protein | protein | 97 | 38% helix, 34% strand | Q471R3 |
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 | 158 | 0.59 | 0.82 | 24 | empty |
| 2 | 53 | 0.26 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1742 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2IFX · Crystal structure of a putative 4-methylmuconolactone methylisomerase (YP_295714.1) from… · 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 Q471R3
- Elsewhere: RCSB PDB 2IFX · PDBe 2IFX · UniProt Q471R3
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