Research workbench
Crystal structure of edds lyase in complex with formate
Analyse Crystal structure of edds lyase in complex with formate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G3E
- Type
- protein
- Length
- 497 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Argininosuccinate lyase
- UniProt
- Q11KV9
- Ligands
- NA
- Pockets
- 7 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Argininosuccinate lyase | protein | 497 | 69% helix, 4% strand | Q11KV9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.48 | 0.78 | 24 | empty |
| 2 | 94 | 0.43 | 0.78 | 18 | empty |
| 3 | 83 | 0.38 | 0.77 | 15 | empty |
| 4 | 74 | 0.37 | 0.77 | 16 | empty |
| 5 | 73 | 0.32 | 0.74 | 12 | empty |
Compared structures
- 6G3E · Crystal structure of EDDS lyase in complex with formate · 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 Q11KV9
- Elsewhere: RCSB PDB 6G3E · PDBe 6G3E · UniProt Q11KV9
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