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Crystal structure of escherichia COLI moea
Analyse Crystal structure of escherichia COLI moea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G8L
- Type
- protein
- Length
- 806 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Molybdopterin biosynthesis moea protein
- UniProt
- P12281
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Molybdopterin biosynthesis moea protein | protein | 403 | 22% helix, 32% strand | P12281 |
Ligands and binding sites
- GOL · Glycerol · additive · 18 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 917 | 0.78 | 0.81 | 94 | GOL |
| 2 | 873 | 0.75 | 0.79 | 73 | GOL |
| 3 | 781 | 0.70 | 0.76 | 79 | GOL |
| 4 | 182 | 0.52 | 0.78 | 21 | empty |
| 5 | 106 | 0.44 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2209 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
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 P12281
- Elsewhere: RCSB PDB 1G8L · PDBe 1G8L · UniProt P12281
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