Research workbench
Crystal structure of a POU/HMG/DNA ternary complex
Analyse Crystal structure of a POU/HMG/DNA ternary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GT0
- Type
- protein + DNA
- Length
- 264 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14859, P48432
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | dna | 24 | — | — |
| B | — | dna | 24 | — | — |
| C | — | protein | 137 | — | P14859 |
| D | — | protein | 79 | — | P48432 |
Compared structures
- 1GT0 · Crystal structure of a POU/HMG/DNA ternary complex · the same entry in another collection · chain A against A, TM-score 1.00
- P48432 · AlphaFold monomer V2.0 prediction for transcription factor sox-2 (P48432) · a predicted model of the same protein · chain D against A, TM-score 0.95
- P14859 · AlphaFold monomer V2.0 prediction for pou domain, class 2, transcription factor 1 (P14859) · a predicted model of the same protein · chain C against A, TM-score 0.92
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 P14859
- Every structure of UniProt P48432
- Elsewhere: RCSB PDB 1GT0 · PDBe 1GT0 · UniProt P14859 · UniProt P48432
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