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Nifs-like protein

Analyse Nifs-like protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EG5
Type: protein
Length: 729 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminotransferase
UniProt: Q9X218
Ligands: PLP, SO4
Pockets: 5 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminotransferase	protein	364	43% helix, 16% strand	Q9X218
B	Aminotransferase	protein	365	44% helix, 16% strand	Q9X218

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

5 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	237	0.72	0.87	22	empty
2	394	0.70	0.82	52	SO4, PLP
3	374	0.68	0.81	46	SO4, PLP
4	78	0.37	0.77	16	empty
5	59	0.35	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 2489 Å² buried · 33 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 modified, 2 cofactor (engineered, pyridoxal phosphate Schiff base).

Compared structures

1EG5 · Nifs-like protein · 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 Q9X218
Elsewhere: RCSB PDB 1EG5 · PDBe 1EG5 · UniProt Q9X218

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