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Crystal structure of mycobacterium tuberculosis argc apoenzyme

Analyse Crystal structure of mycobacterium tuberculosis argc apoenzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NNI
Type: protein
Length: 688 residues
Chains: 2
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: P9WPZ9
Pockets: 7 · best druggability 0.67

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38)	protein	344	33% helix, 22% strand	P9WPZ9

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	421	0.67	0.79	38	empty
2	315	0.64	0.80	51	empty
3	537	0.63	0.75	62	empty
4	307	0.61	0.79	53	empty
5	102	0.44	0.78	20	empty

Interfaces

1 interface between chains.

A–B · 1194 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7NNI · Crystal structure of Mycobacterium tuberculosis ArgC apoenzyme · the same entry in another collection · chain A against A, TM-score 1.00
P9WPZ9 · AlphaFold monomer V2.0 prediction for N-acetyl-gamma-glutamyl- phosphate reductase… · a predicted model of the same protein · 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 P9WPZ9
Elsewhere: RCSB PDB 7NNI · PDBe 7NNI · UniProt P9WPZ9

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