Research workbench
Dimerization domain of hnf-1ALPHA with a leu 13 selenomethionine substitution
Analyse Dimerization domain of hnf-1ALPHA with a leu 13 selenomethionine substitution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G2Z
- Type
- protein
- Length
- 63 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hepatocyte nuclear factor 1-alpha
- UniProt
- P22361
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte nuclear factor 1-alpha | protein | 32 | 72% helix, 0% strand | P22361 |
| B | Hepatocyte nuclear factor 1-alpha | protein | 31 | 77% helix, 0% strand | P22361 |
Interfaces
1 interface between chains.
- A–B · 378 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 1G2Z · Dimerization domain of hnf-1ALPHA with a leu 13 selenomethionine substitution · the same entry in another collection · chain A against A, TM-score 1.00
- P22361 · AlphaFold monomer V2.0 prediction for hepatocyte nuclear factor 1-alpha (P22361) · a predicted model of the same protein · chain B against A, TM-score 0.59
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 P22361
- Elsewhere: RCSB PDB 1G2Z · PDBe 1G2Z · UniProt P22361
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