Research workbench
Crystal structure of GH3.12 in complex with AMP and salicylate
Analyse Crystal structure of GH3.12 in complex with AMP and salicylate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EQL
- Type
- protein
- Length
- 973 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9LYU4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 494 | — | Q9LYU4 |
| B | — | protein | 479 | — | Q9LYU4 |
Compared structures
- 4EQL · Crystal Structure of GH3.12 in complex with AMP and salicylate · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LYU4 · AlphaFold monomer V2.0 prediction for 4-substituted benzoates- glutamate ligase GH3.12… · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q9LYU4
- Elsewhere: RCSB PDB 4EQL · PDBe 4EQL · UniProt Q9LYU4
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