Research workbench

ALPHA/BETA hydrolase fold protein of unknown function

Analyse ALPHA/BETA hydrolase fold protein of unknown function in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Q0X
Type: protein
Length: 587 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q389W3
Pockets: 6 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	294	42% helix, 21% strand	Q389W3
B	Uncharacterized protein	protein	293	41% helix, 20% strand	Q389W3

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

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	194	0.73	0.89	31	GOL
2	124	0.69	0.90	29	GOL
3	247	0.52	0.75	28	empty
4	171	0.45	0.75	23	empty
5	76	0.36	0.77	20	empty

Interfaces

1 interface between chains.

A–B · 2121 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

2Q0X · Alpha/Beta hydrolase fold protein of unknown function · 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 Q389W3
Elsewhere: RCSB PDB 2Q0X · PDBe 2Q0X · UniProt Q389W3

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