MolNFT v1 · #39731 · protein

Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (RV1652) from mycobacterium tuberculosis

2I3A: “Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (RV1652) from mycobacterium tuberculosis”. X-ray diffraction, 20 pockets (best druggability 0.82). MolNFT v1 #39731 on GenesisL1: 3D structure, binding sites and…

PDB: 2I3A
Type: protein
Length: 1,381 residues
Chains: 4
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: P63562
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 32% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38)	protein	344	32% helix, 22% strand	P63562
B	N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38)	protein	346	32% helix, 23% strand	P63562
D	N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38)	protein	347	33% helix, 21% strand	P63562

Ligands and binding sites

BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	204	0.82	0.96	33	empty
2	1031	0.81	0.83	126	empty
3	612	0.69	0.78	69	empty
4	436	0.68	0.80	42	empty
5	551	0.68	0.78	50	empty

Interfaces

6 interfaces between chains.

B–C · 1751 Å² buried · 15 hydrogen bonds · protein-protein
A–D · 1740 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 1176 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 1156 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 735 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

2I3A · Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) 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 P63562
Elsewhere: RCSB PDB 2I3A · PDBe 2I3A · UniProt P63562

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