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Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TTHA1904) from thermus thermophilus

Analyse Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TTHA1904)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OZP
Type: protein
Length: 342 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetyl-gamma-glutamyl-phosphate reductase
EC: 1.2.1.38
UniProt: Q5SH26
Ligands: AZI, SO4
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38)	protein	342	33% helix, 22% strand	Q5SH26

Ligands and binding sites

AZI · Azide ion · ion · 7 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

3 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	395	0.67	0.80	46	SO4, AZI
2	80	0.33	0.75	17	empty
3	58	0.32	0.76	12	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

2OZP · Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TTHA1904) from Thermus… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5SH26
Elsewhere: RCSB PDB 2OZP · PDBe 2OZP · UniProt Q5SH26

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