MolNFT v1 · #151341 · protein

Crystal structure of farnesoid X receptor (fxr) with bound ncoa-2 peptide

6HL0 · Bile acid receptor: “Crystal structure of farnesoid X receptor (fxr) with bound ncoa-2 peptide”. X-ray diffraction, 3 pockets (best druggability 0.84). MolNFT v1 #151341 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HL0
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile acid receptor; Ncoa-2 peptide (nuclear receptor coactivator 2), lys-glu…
UniProt: Q96RI1
Pockets: 3 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bile acid receptor	protein	231	74% helix, 0% strand	Q96RI1
B	Ncoa-2 peptide (nuclear receptor coactivator 2), lys-glu- asn-ala-leu-leu-arg-tyr-leu-leu-asp-lys-asp	protein	13	54% helix, 0% strand	—

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	199	0.84	0.97	26	empty
2	130	0.40	0.75	19	empty
3	65	0.38	0.79	14	empty

Interfaces

1 interface between chains.

A–B · 562 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6HL0 · Crystal Structure of Farnesoid X receptor (FXR) with bound NCoA-2 peptide · the same entry in another collection · chain A against A, TM-score 1.00

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 Q96RI1
Elsewhere: RCSB PDB 6HL0 · PDBe 6HL0 · UniProt Q96RI1

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