MolNFT v1 · #106251 · protein + DNA
Complex of escherichia COLI DNA adenine methyltransferase (dam) with adomet and with DNA containing proximal pap regulon sequence
4RTP · DNA adenine methylase: “Complex of escherichia COLI DNA adenine methyltransferase (dam) with adomet and with DNA containing proximal…”. X-ray diffraction, 1 ligand (SAM), 1 pocket (best druggability 0.54). MolNFT v1 #106251 on…
- PDB
- 4RTP
- Type
- protein + DNA
- Length
- 268 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA adenine methylase; DNA (5'-D(*TP*TP*TP*AP*AP*AP*GP*AP*TP*CP*G)-3'); DNA…
- UniProt
- H0Q7C9
- Ligands
- SAM
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA adenine methylase | protein | 246 | 43% helix, 17% strand | H0Q7C9 |
| F | DNA (5'-D(*TP*TP*TP*AP*AP*AP*GP*AP*TP*CP*G)-3') | dna | 11 | — | — |
| G | DNA (5'-D(*AP*CP*GP*AP*TP*CP*TP*TP*TP*AP*A)-3') | dna | 11 | — | — |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.54 | 0.78 | 32 | SAM |
Interfaces
3 interfaces between chains.
- F–G · 442 Ų buried · 43 hydrogen bonds · nucleic-nucleic
- A–F · 301 Ų buried · 8 hydrogen bonds · protein-nucleic
- A–G · 37 Ų buried · 0 hydrogen bonds · protein-nucleic
Compared structures
- 4RTP · Complex of Escherichia coli DNA Adenine Methyltransferase (DAM) with AdoMet and with DNA… · the same entry in another collection · chain F against F, 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 H0Q7C9
- Elsewhere: RCSB PDB 4RTP · PDBe 4RTP · UniProt H0Q7C9
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