MolNFT v1 · #147976 · protein
The structure of the mo-insertase domain CNX1E from arabidopsis thaliana in complex with AMP
6ETD: “The structure of the mo-insertase domain CNX1E from arabidopsis thaliana in complex with AMP”. X-ray diffraction, 3 ligands (ACE, AMP, MG). MolNFT v1 #147976 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ETD
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q39054
- Ligands
- ACE, AMP, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 419 | — | Q39054 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A
- AMP · Adenosine monophosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ETD · The Structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q39054 · AlphaFold monomer V2.0 prediction for molybdopterin biosynthesis protein CNX1 (Q39054) · a predicted model of the same protein · 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 Q39054
- Elsewhere: RCSB PDB 6ETD · PDBe 6ETD · UniProt Q39054
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