Research workbench
Structure of nucleic-acid binding protein
Analyse Structure of nucleic-acid binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q2K
- Type
- protein + DNA
- Length
- 109 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-D(*AP*GP*TP*AP*TP*AP*(5IU)P*AP*CP*(5IU) P*AP*GP*TP*AP*TP*AP*TP*AP*CP*T)-3')…
- UniProt
- Q2FDA3
Structure
x-ray diffraction · 3 distinct chains · 51% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | DNA (5'-D(*AP*GP*TP*AP*TP*AP*(5IU)P*AP*CP*(5IU) P*AP*GP*TP*AP*TP*AP*TP*AP*CP*T)-3') | dna | 20 | — | — |
| A | Hypothetical protein | protein | 45 | 49% helix, 20% strand | Q2FDA3 |
| B | Hypothetical protein | protein | 44 | 52% helix, 20% strand | Q2FDA3 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1979 Ų buried · 21 hydrogen bonds · protein-protein
- F–A · 314 Ų buried · 9 hydrogen bonds · protein-nucleic
- F–B · 288 Ų buried · 5 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 2 modified (nucleotide modification).
Compared structures
- 2Q2K · Structure of nucleic-acid binding protein · 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 Q2FDA3
- Elsewhere: RCSB PDB 2Q2K · PDBe 2Q2K · UniProt Q2FDA3
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