Research workbench
Triuret hydrolase (trta) from herbaspirillum sp. bh-1 C162S bound with biuret
Analyse Triuret hydrolase (trta) from herbaspirillum sp. bh-1 C162S bound with biuret in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XJ4
- Type
- protein
- Length
- 877 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2N6JFX7
- Ligands
- C5J
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 219 | — | A0A2N6JFX7 |
| D | — | protein | 220 | — | A0A2N6JFX7 |
Ligands and binding sites
- C5J · dicarbonimidic diamide · ligand · chains A, B
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XJ4 · Triuret Hydrolase (TrtA) from Herbaspirillum sp. BH-1 C162S bound with biuret · 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 A0A2N6JFX7
- Elsewhere: RCSB PDB 6XJ4 · PDBe 6XJ4 · UniProt A0A2N6JFX7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.