Research workbench
Crystal structure of type-II log from corynebacterium glutamicum
Analyse Crystal structure of type-II log from corynebacterium glutamicum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WQ3
- Type
- protein
- Length
- 620 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1B4WK77
- Ligands
- CL, PO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 206 | — | A0A1B4WK77 |
| B | — | protein | 206 | — | A0A1B4WK77 |
| C | — | protein | 208 | — | A0A1B4WK77 |
Ligands and binding sites
- CL · Chloride ion · ion · 5 copies · chains B, C
- PO4 · Phosphate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains B, C
- 1PE · Pentaethylene glycol · additive · chains A
- GOL · Glycerol · additive · chains A
- PGE · Triethylene glycol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WQ3 · Crystal structure of type-II LOG from Corynebacterium glutamicum · 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 A0A1B4WK77
- Elsewhere: RCSB PDB 5WQ3 · PDBe 5WQ3 · UniProt A0A1B4WK77
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