Research workbench

Transcription factor grdbd and gre complex

Analyse Transcription factor grdbd and gre complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EMQ
Type: protein + DNA
Length: 178 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA (5'- D(*CP*CP*AP*GP*AP*AP*CP*AP*TP*GP*AP*TP*GP*TP*TP*CP*TP*G)-3'); DNA (5'…
UniProt: P04150
Ligands: ZN
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 4 distinct chains · 34% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	DNA (5'- D(CPCPAPGPAPAPCPAPTPGPAPTPGPTPTPCPTPG)-3')	dna	18	—	—
D	DNA (5'- D(CPCPAPGPAPAPCPAPTPCPAPTPGPTPTPCPTPG)-3')	dna	18	—	—
A	Glucocorticoid receptor	protein	70	36% helix, 11% strand	P04150
B	Glucocorticoid receptor	protein	72	32% helix, 11% strand	P04150

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	504	0.68	0.79	47	empty
2	82	0.36	0.76	17	empty
3	70	0.30	0.74	18	empty

Interfaces

6 interfaces between chains.

C–D · 791 Å² buried · 71 hydrogen bonds · nucleic-nucleic
A–B · 600 Å² buried · 10 hydrogen bonds · protein-protein
D–A · 364 Å² buried · 6 hydrogen bonds · protein-nucleic
C–A · 345 Å² buried · 6 hydrogen bonds · protein-nucleic
C–B · 335 Å² buried · 8 hydrogen bonds · protein-nucleic

Compared structures

5EMQ · Transcription factor GRDBD and GRE complex · the same entry in another collection · chain C against C, TM-score 1.00
P04150 · AlphaFold monomer V2.0 prediction for glucocorticoid receptor (P04150) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P04150
Elsewhere: RCSB PDB 5EMQ · PDBe 5EMQ · UniProt P04150

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