Research workbench
DNA bound structure of the N-terminal domain of abrb
Analyse DNA bound structure of the N-terminal domain of abrb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K1N
- Type
- protein + DNA
- Length
- 270 residues
- Chains
- 6
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (25-mer); Abrb family transcriptional regulator
- UniProt
- A0A063X7Z2
- Pockets
- 5 · best druggability 0.70
Structure
solution nmr · 3 distinct chains · 15% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | DNA (25-mer) | dna | 25 | — | — |
| F | DNA (25-mer) | dna | 25 | — | — |
| A, B, C, D | Abrb family transcriptional regulator | protein | 55 | 15% helix, 35% strand | A0A063X7Z2 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.70 | 0.92 | 30 | empty |
| 2 | 323 | 0.54 | 0.75 | 39 | empty |
| 3 | 64 | 0.41 | 0.80 | 21 | empty |
| 4 | 120 | 0.39 | 0.76 | 20 | empty |
| 5 | 101 | 0.35 | 0.75 | 18 | empty |
Interfaces
14 interfaces between chains.
- C–D · 1991 Ų buried · 43 hydrogen bonds · protein-protein
- A–B · 1774 Ų buried · 32 hydrogen bonds · protein-protein
- E–F · 1074 Ų buried · 71 hydrogen bonds · nucleic-nucleic
- F–C · 445 Ų buried · 13 hydrogen bonds · protein-nucleic
- E–D · 422 Ų buried · 7 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2K1N · DNA bound structure of the N-terminal domain of AbrB · the same entry in another collection · chain E against E, 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 A0A063X7Z2
- Elsewhere: RCSB PDB 2K1N · PDBe 2K1N · UniProt A0A063X7Z2
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