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Wild-type hnf-1ALPHA dimerization domain

Analyse Wild-type hnf-1ALPHA dimerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G39
Type: protein
Length: 117 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hepatocyte nuclear factor 1-alpha
UniProt: P22361

Structure

x-ray diffraction · 3 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hepatocyte nuclear factor 1-alpha	protein	28	71% helix, 0% strand	P22361
B, D	Hepatocyte nuclear factor 1-alpha	protein	30	77% helix, 0% strand	P22361
C	Hepatocyte nuclear factor 1-alpha	protein	29	72% helix, 0% strand	P22361

Interfaces

6 interfaces between chains.

B–D · 738 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 607 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 400 Å² buried · 1 hydrogen bond · protein-protein
C–D · 392 Å² buried · 1 hydrogen bond · protein-protein
A–D · 205 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1G39 · Wild-type hnf-1ALPHA dimerization domain · 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 C against A, TM-score 0.71

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 1G39 · PDBe 1G39 · UniProt P22361

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