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Crystal structure of the wild human ror gamma ligand binding domain.

Analyse Crystal structure of the wild human ror gamma ligand binding domain. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5X8U
Type: protein
Length: 253 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor ror-gamma; Nuclear receptor coactivator 1
EC: 2.3.1.48
UniProt: P51449, Q15788
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear receptor ror-gamma	protein	244	73% helix, 4% strand	P51449
B	Nuclear receptor coactivator 1 (EC 2.3.1.48)	protein	9	78% helix, 0% strand	Q15788

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	364	0.82	0.90	36	empty
2	238	0.58	0.79	33	empty
3	58	0.46	0.84	15	empty
4	74	0.37	0.78	17	empty

Interfaces

1 interface between chains.

A–B · 493 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5X8U · Crystal Structure of the wild Human ROR gamma Ligand Binding Domain. · 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 P51449
Every structure of UniProt Q15788
Elsewhere: RCSB PDB 5X8U · PDBe 5X8U · UniProt P51449 · UniProt Q15788

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