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Structure of nagst-1

Analyse Structure of nagst-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ON7
Type: protein
Length: 824 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Na glutathione S-transferase 1
Pockets: 8 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Na glutathione S-transferase 1	protein	206	58% helix, 9% strand	—

Pockets

8 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	1066	0.81	0.82	86	empty
2	1069	0.80	0.81	82	empty
3	276	0.55	0.76	20	empty
4	181	0.46	0.76	28	empty
5	118	0.41	0.76	21	empty

Interfaces

5 interfaces between chains.

A–D · 1347 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 1333 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 229 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 151 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 56 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2ON7 · Structure of NaGST-1 · 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
Elsewhere: RCSB PDB 2ON7 · PDBe 2ON7

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