Research workbench

Glucocorticoid receptor MUTANT/DNA complex

Analyse Glucocorticoid receptor MUTANT/DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LAT
Type: protein + DNA
Length: 183 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA (5'- D(*TP*TP*CP*CP*AP*GP*AP*AP*CP*AP*TP*GP*TP*TP*CP*TP*G P*GP*A)-3'); Glucocorticoid…
UniProt: P06536
Ligands: ZN
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 32% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, D	DNA (5'- D(TPTPCPCPAPGPAPAPCPAPTPGPTPTPCPTPG PGP*A)-3')	dna	19	—	—
A	Glucocorticoid receptor	protein	71	31% helix, 11% strand	P06536
B	Glucocorticoid receptor	protein	74	34% helix, 11% strand	P06536

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	412	0.59	0.76	50	empty
2	74	0.42	0.80	15	empty
3	60	0.37	0.79	12	empty

Interfaces

5 interfaces between chains.

C–D · 818 Å² buried · 73 hydrogen bonds · nucleic-nucleic
D–A · 434 Å² buried · 11 hydrogen bonds · protein-nucleic
C–B · 429 Å² buried · 6 hydrogen bonds · protein-nucleic
D–B · 415 Å² buried · 10 hydrogen bonds · protein-nucleic
C–A · 291 Å² buried · 7 hydrogen bonds · protein-nucleic

Compared structures

1LAT · Glucocorticoid receptor MUTANT/DNA complex · the same entry in another collection · chain C against C, TM-score 1.00
P06536 · AlphaFold monomer V2.0 prediction for glucocorticoid receptor (P06536) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 P06536
Elsewhere: RCSB PDB 1LAT · PDBe 1LAT · UniProt P06536

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