Research workbench
Cama adenine methyltransferase complexed to cognate substrate DNA and inhibitor SGC0946
Analyse Cama adenine methyltransferase complexed to cognate substrate DNA and inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RFL
- Type
- protein + DNA
- Length
- 1,734 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q183J3
- Ligands
- AW2, K
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 552 | — | Q183J3 |
| B | — | protein | 556 | — | Q183J3 |
| C | — | protein | 543 | — | Q183J3 |
| E | — | dna | 13 | — | — |
| D, F, H | — | dna | 14 | — | — |
| G, I | — | dna | 14 | — | — |
Ligands and binding sites
- AW2 · 5-bromo-7-{5-[(3-{[(4-tert-butylphenyl) carbamoyl]amino}propyl)(propan-2-yl)amino]-5-deoxy-beta-D-ribofuranosyl}-7H-pyrrolo[2,3-d]pyrimidin-4-amine · ligand · 3 copies · chains A, D, B, F, C, H
- K · Potassium ion · metal · 5 copies · chains A, B, C
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B, F, C, E, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7RFL · CamA Adenine Methyltransferase Complexed to Cognate Substrate DNA and Inhibitor SGC0946 · the same entry in another collection · chain G against G, 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 7RFL · PDBe 7RFL · UniProt Q183J3
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