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The 2.0 ångström crystal structure of predicted glutamine amidotransferase from pseudomonas aeruginosa PA01

Analyse The 2.0 ångström crystal structure of predicted glutamine amidotransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TE5
Type: protein
Length: 506 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Conserved hypothetical protein
UniProt: Q9I437
Pockets: 7 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Conserved hypothetical protein	protein	253	17% helix, 40% strand	Q9I437

Pockets

7 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	247	0.81	0.93	45	empty
2	165	0.58	0.83	28	empty
3	87	0.49	0.82	19	empty
4	83	0.46	0.81	21	empty
5	65	0.44	0.82	14	empty

Interfaces

1 interface between chains.

A–B · 1421 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1TE5 · The 2.0 Angstrom crystal structure of predicted glutamine amidotransferase from… · 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 Q9I437
Elsewhere: RCSB PDB 1TE5 · PDBe 1TE5 · UniProt Q9I437 · AlphaFold DB Q9I437

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