Research workbench

Putrescine transaminase from Pseudomonas putida

Analyse Putrescine transaminase from Pseudomonas putida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HX9
Type: protein
Length: 767 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.05
Source: Pseudomonas putida
Molecule: Aspartate aminotransferase family protein
UniProt: A0A1X0Z7H5
Pockets: 11 · best druggability 0.64

Structure

x-ray diffraction · resolution 2.05 · 2 distinct chains · 44% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Aspartate aminotransferase family protein	protein	383	44% helix, 22% strand	A0A1X0Z7H5
A	Aspartate aminotransferase family protein	protein	384	44% helix, 21% strand	A0A1X0Z7H5

Pockets

11 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	383	0.64	0.78	52	empty
2	240	0.59	0.80	34	empty
3	93	0.43	0.79	23	empty
4	66	0.42	0.80	16	empty
5	62	0.41	0.81	17	empty

Interfaces

1 interface between chains.

B–A · 2145 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

6HX9 · Putrescine transaminase from pseudomonas putida · 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 A0A1X0Z7H5
Elsewhere: RCSB PDB 6HX9 · PDBe 6HX9 · UniProt A0A1X0Z7H5

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