MolNFT v1 · #169659 · protein
Triuret hydrolase (trta) from herbaspirillum sp. bh-1 C162S bound with triuret
6XJE: “Triuret hydrolase (trta) from herbaspirillum sp. bh-1 C162S bound with triuret”. X-ray diffraction, 1 ligand (TIU). MolNFT v1 #169659 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XJE
- Type
- protein
- Length
- 878 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2N6JFX7
- Ligands
- TIU
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 219 | — | A0A2N6JFX7 |
| B, D | — | protein | 220 | — | A0A2N6JFX7 |
Ligands and binding sites
- TIU · tricarbonodiimidic diamide · ligand · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XJE · Triuret Hydrolase (TrtA) from Herbaspirillum sp. BH-1 C162S bound with triuret · the same entry in another collection · chain C against C, 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 6XJE · PDBe 6XJE · UniProt A0A2N6JFX7
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