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Crystal structure of a single-chain E/F type bilin lyase-isomerase mpeq in space group C2221
Analyse Crystal structure of a single-chain E/F type bilin lyase-isomerase mpeq in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MCH
- Type
- protein
- Length
- 808 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bilin lyase-isomerase
- UniProt
- U3MW57
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bilin lyase-isomerase | protein | 404 | 70% helix, 1% strand | U3MW57 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 579 | 0.73 | 0.81 | 54 | empty |
| 2 | 352 | 0.69 | 0.82 | 33 | empty |
| 3 | 126 | 0.51 | 0.80 | 26 | empty |
| 4 | 61 | 0.33 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2616 Ų buried · 48 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 7MCH · Crystal structure of a single-chain E/F type bilin lyase-isomerase MpeQ in space group… · 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 U3MW57
- Elsewhere: RCSB PDB 7MCH · PDBe 7MCH · UniProt U3MW57
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