MolNFT v1 · #186484 · protein + DNA
Cama adenine methyltransferase complexed to cognate substrate DNA and inhibitor sinefungin
7RFK: “Cama adenine methyltransferase complexed to cognate substrate DNA and inhibitor sinefungin”. X-ray diffraction, 1 ligand (K). MolNFT v1 #186484 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7RFK
- Type
- protein + DNA
- Length
- 1,791 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q183J3
- Ligands
- K
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 569 | — | Q183J3 |
| B | — | protein | 576 | — | Q183J3 |
| C | — | protein | 563 | — | Q183J3 |
| E | — | dna | 13 | — | — |
| D, F, H | — | dna | 14 | — | — |
| G, I | — | dna | 14 | — | — |
Ligands and binding sites
- K · Potassium ion · metal · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 24 copies · chains A, E, B, C, H, F, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7RFK · CamA Adenine Methyltransferase Complexed to Cognate Substrate DNA and Inhibitor Sinefungin · 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 7RFK · PDBe 7RFK · UniProt Q183J3
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