Research workbench

Spua mutant - H221N with glutamyl-thioester

Analyse Spua mutant - H221N with glutamyl-thioester in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D50
Type: protein
Length: 503 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable glutamine amidotransferase
UniProt: Q9I6J4
Ligands: MG
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable glutamine amidotransferase	protein	248	33% helix, 25% strand	Q9I6J4
B	Probable glutamine amidotransferase	protein	255	32% helix, 24% strand	Q9I6J4

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

3 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	312	0.61	0.79	53	empty
2	289	0.58	0.78	45	empty
3	129	0.48	0.79	23	empty

Interfaces

1 interface between chains.

A–B · 1649 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

7D50 · SpuA mutant - H221N with glutamyl-thioester · 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 Q9I6J4
Elsewhere: RCSB PDB 7D50 · PDBe 7D50 · UniProt Q9I6J4

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