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Crystal structure of the apo-state of porcine OAS1

Analyse Crystal structure of the apo-state of porcine OAS1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RWQ
Type: protein
Length: 692 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2'-5'-oligoadenylate synthase 1
EC: 2.7.7.84
UniProt: Q29599
Pockets: 7 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	2'-5'-oligoadenylate synthase 1 (EC 2.7.7.84)	protein	346	45% helix, 14% strand	Q29599

Pockets

7 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	788	0.81	0.84	80	empty
2	791	0.76	0.80	72	empty
3	703	0.74	0.80	68	empty
4	85	0.33	0.74	16	empty
5	63	0.33	0.76	10	empty

Interfaces

1 interface between chains.

A–B · 713 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4RWQ · Crystal structure of the apo-state of porcine OAS1 · the same entry in another collection · chain A against A, TM-score 1.00
Q29599 · AlphaFold monomer V2.0 prediction for 2'-5'-oligoadenylate synthase 1 (Q29599) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q29599
Elsewhere: RCSB PDB 4RWQ · PDBe 4RWQ · UniProt Q29599

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