Research workbench

Structure and function of the B/HLH/Z domain of usf

Analyse Structure and function of the B/HLH/Z domain of usf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AN4
Type: protein + DNA
Length: 172 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA (5'- D(*CP*AP*CP*CP*CP*GP*GP*TP*CP*AP*CP*GP*TP*GP*GP*CP*C P*TP*AP*CP*A)- 3'); DNA…
UniProt: P22415
Pockets: 6 · best druggability 0.84

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	DNA (5'- D(CPAPCPCPCPGPGPTPCPAPCPGPTPGPGPCPC PTPAPCP*A)- 3')	dna	21	—	—
D	DNA (5'- D(GPTPGPTPAPGPGPCPCPAPCPGPTPGPAPCPC PGPGPGP*T)- 3')	dna	21	—	—
A, B	Protein (upstream stimulatory factor)	protein	65	45% helix, 0% strand	P22415

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	468	0.84	0.91	56	empty
2	194	0.56	0.80	20	empty
3	183	0.50	0.78	20	empty
4	220	0.48	0.75	25	empty
5	168	0.40	0.73	21	empty

Interfaces

6 interfaces between chains.

C–D · 960 Å² buried · 104 hydrogen bonds · nucleic-nucleic
A–B · 782 Å² buried · 4 hydrogen bonds · protein-protein
C–B · 462 Å² buried · 11 hydrogen bonds · protein-nucleic
C–A · 422 Å² buried · 9 hydrogen bonds · protein-nucleic
D–A · 392 Å² buried · 11 hydrogen bonds · protein-nucleic

Compared structures

1AN4 · Structure and function of the B/HLH/Z domain of usf · the same entry in another collection · chain C against C, TM-score 1.00
P22415 · AlphaFold monomer V2.0 prediction for upstream stimulatory factor 1 (P22415) · a predicted model of the same protein · chain A against A, TM-score 0.54

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 P22415
Elsewhere: RCSB PDB 1AN4 · PDBe 1AN4 · UniProt P22415

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