Research workbench
Crystal structure of a hmg domain of transcription factor sox-9 bound to DNA (sox-9/DNA) from homo sapiens at 2.77 a resolution
Analyse Crystal structure of a hmg domain of transcription factor sox-9 bound to DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EUW
- Type
- protein + DNA
- Length
- 96 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor sox-9; DNA (5'-D(*CP*TP*CP*TP*TP*TP*GP*AP*GP*AP*AP*G)-3'); DNA…
- UniProt
- P48436
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 3 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription factor sox-9 | protein | 72 | 68% helix, 0% strand | P48436 |
| B | DNA (5'-D(*CP*TP*CP*TP*TP*TP*GP*AP*GP*AP*AP*G)-3') | dna | 12 | — | — |
| C | DNA (5'-D(*CP*TP*TP*CP*TP*CP*AP*AP*AP*GP*AP*G)-3') | dna | 12 | — | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.44 | 0.81 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 609 Ų buried · 12 hydrogen bonds · protein-nucleic
- A–C · 596 Ų buried · 10 hydrogen bonds · protein-nucleic
- B–C · 537 Ų buried · 55 hydrogen bonds · nucleic-nucleic
Compared structures
- 4EUW · Crystal structure of a HMG domain of transcription factor SOX-9 bound to DNA (SOX-9/DNA)… · the same entry in another collection · chain A against A, TM-score 1.00
- P48436 · AlphaFold monomer V2.0 prediction for transcription factor sox-9 (P48436) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P48436
- Elsewhere: RCSB PDB 4EUW · PDBe 4EUW · UniProt P48436
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