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Crystal structure of mle D178N variant
Analyse Crystal structure of mle D178N variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F9C
- Type
- protein
- Length
- 720 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (muconate cycloisomerase I)
- EC
- 5.5.1.1
- UniProt
- Q51958
- Ligands
- MN
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (muconate cycloisomerase I) (EC 5.5.1.1) | protein | 360 | 42% helix, 22% strand | Q51958 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 797 | 0.78 | 0.81 | 78 | empty |
| 2 | 214 | 0.55 | 0.78 | 40 | empty |
| 3 | 153 | 0.55 | 0.81 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 903 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1F9C · Crystal structure of mle D178N variant · 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 Q51958
- Elsewhere: RCSB PDB 1F9C · PDBe 1F9C · UniProt Q51958
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