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Crystal structure of a complex between the dimerization domain of hnf-1 alpha and the coactivator dcoh

Analyse Crystal structure of a complex between the dimerization domain of hnf-1 alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1F93
Type: protein
Length: 512 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dimerization cofactor of hepatocyte nuclear factor 1-alpha; Hepatocyte nuclear factor…
UniProt: P61459, P22361
Pockets: 4 · best druggability 0.42

Structure

x-ray diffraction · 8 distinct chains · 51% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dimerization cofactor of hepatocyte nuclear factor 1-alpha	protein	103	45% helix, 20% strand	P61459
B	Dimerization cofactor of hepatocyte nuclear factor 1-alpha	protein	99	51% helix, 23% strand	P61459
C	Dimerization cofactor of hepatocyte nuclear factor 1-alpha	protein	99	45% helix, 21% strand	P61459
D	Dimerization cofactor of hepatocyte nuclear factor 1-alpha	protein	100	45% helix, 21% strand	P61459
E	Hepatocyte nuclear factor 1-alpha	protein	31	61% helix, 0% strand	P22361
F	Hepatocyte nuclear factor 1-alpha	protein	27	70% helix, 0% strand	P22361
G	Hepatocyte nuclear factor 1-alpha	protein	27	70% helix, 0% strand	P22361
H	Hepatocyte nuclear factor 1-alpha	protein	26	73% helix, 0% strand	P22361

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	182	0.42	0.73	22	empty
2	77	0.35	0.76	16	empty
3	58	0.31	0.76	15	empty
4	57	0.28	0.74	12	empty

Interfaces

13 interfaces between chains.

E–F · 743 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 735 Å² buried · 10 hydrogen bonds · protein-protein
G–H · 728 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 707 Å² buried · 5 hydrogen bonds · protein-protein
B–E · 447 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

1F93 · Crystal structure of a complex between the dimerization domain of hnf-1 alpha and the… · the same entry in another collection · chain H against H, TM-score 1.00
P61459 · AlphaFold monomer V2.0 prediction for pterin-4-alpha-carbinolamine dehydratase (P61459) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P61459
Every structure of UniProt P22361
Elsewhere: RCSB PDB 1F93 · PDBe 1F93 · UniProt P61459 · UniProt P22361

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