MolNFT v1 · #181378 · protein + DNA
Cama adenine methyltransferase complexed to cognate substrate DNA and cofactor sah
7LT5: “Cama adenine methyltransferase complexed to cognate substrate DNA and cofactor sah”. X-ray diffraction. MolNFT v1 #181378 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7LT5
- Type
- protein + DNA
- Length
- 1,790 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q183J3
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 569 | — | Q183J3 |
| B | — | protein | 577 | — | Q183J3 |
| C | — | protein | 561 | — | Q183J3 |
| E | — | dna | 13 | — | — |
| D, F, H | — | dna | 14 | — | — |
| G, I | — | dna | 14 | — | — |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, B, C, D, G, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LT5 · CamA Adenine Methyltransferase Complexed to Cognate Substrate DNA and Cofactor SAH · the same entry in another collection · chain I against I, 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 Q183J3
- Elsewhere: RCSB PDB 7LT5 · PDBe 7LT5 · UniProt Q183J3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.