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2.0 ångström crystal structure of glutamate--cysteine ligase (gsha) ftom francisella tularensis in complex with AMP

Analyse 2.0 ångström crystal structure of glutamate--cysteine ligase (gsha) ftom… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NZT
Type: protein
Length: 498 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate--cysteine ligase
EC: 6.3.2.2
UniProt: Q5NHS8
Ligands: AMP, SO4
Pockets: 4 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate--cysteine ligase (EC 6.3.2.2)	protein	498	50% helix, 13% strand	Q5NHS8

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
SO4 · Sulfate ion · ion · 11 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1025	0.86	0.86	74	SO4
2	66	0.39	0.80	17	SO4
3	67	0.36	0.77	15	empty
4	59	0.27	0.73	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3NZT · 2.0 Angstrom Crystal structure of Glutamate--Cysteine Ligase (gshA) ftom Francisella… · 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 Q5NHS8
Elsewhere: RCSB PDB 3NZT · PDBe 3NZT · UniProt Q5NHS8

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