Research workbench
Crystal structure of the E.COLI seqa protein complexed with hemimethylated DNA
Analyse Crystal structure of the E.COLI seqa protein complexed with hemimethylated DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IU3
- Type
- protein + DNA
- Length
- 270 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*AP*AP*GP*GP*AP*TP*CP*CP*AP*A)-3'; 5'-D(*TP*TP*GP*GP*AP*TP*CP*CP*TP*T)-3'; Seqa…
- UniProt
- P36658
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 3 distinct chains · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | 5'-D(*AP*AP*GP*GP*AP*TP*CP*CP*AP*A)-3' | dna | 10 | — | — |
| B, E | 5'-D(*TP*TP*GP*GP*AP*TP*CP*CP*TP*T)-3' | dna | 10 | — | — |
| C, F | Seqa protein | protein | 115 | 58% helix, 6% strand | P36658 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.38 | 0.73 | 20 | empty |
| 2 | 89 | 0.34 | 0.75 | 12 | empty |
Interfaces
12 interfaces between chains.
- B–C · 505 Ų buried · 14 hydrogen bonds · protein-nucleic
- E–F · 477 Ų buried · 11 hydrogen bonds · protein-nucleic
- A–B · 429 Ų buried · 45 hydrogen bonds · nucleic-nucleic
- D–E · 425 Ų buried · 41 hydrogen bonds · nucleic-nucleic
- D–F · 424 Ų buried · 7 hydrogen bonds · protein-nucleic
Compared structures
- 1IU3 · Crystal structure of the E.COLI seqa protein complexed with hemimethylated DNA · the same entry in another collection · 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 P36658
- Elsewhere: RCSB PDB 1IU3 · PDBe 1IU3 · UniProt P36658
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