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Saccharomyces cerevisiae GAS2P apostructure (E176Q mutant)

Analyse Saccharomyces cerevisiae GAS2P apostructure (E176Q mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W61
Type: protein
Length: 470 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycolipid-anchored surface protein 2
EC: 2.4.1.-
UniProt: Q06135
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycolipid-anchored surface protein 2 (EC 2.4.1.-)	protein	470	34% helix, 16% strand	Q06135

Pockets

5 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	460	0.62	0.76	56	empty
2	232	0.52	0.76	30	empty
3	124	0.42	0.76	21	empty
4	77	0.34	0.75	17	empty
5	69	0.28	0.72	15	empty

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

2W61 · Saccharomyces cerevisiae Gas2p apostructure (E176Q mutant) · the same entry in another collection · chain A against A, TM-score 1.00
Q06135 · AlphaFold monomer V2.0 prediction for 1,3-beta-glucanosyltransferase GAS2 (Q06135) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q06135
Elsewhere: RCSB PDB 2W61 · PDBe 2W61 · UniProt Q06135

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