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Crystal structure of escherichia COLI mazg, the regulator of nutritional stress response

Analyse Crystal structure of escherichia COLI mazg, the regulator of nutritional stress… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CRA
Type: protein
Length: 461 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein mazg
UniProt: P0AEY3
Pockets: 7 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein mazg	protein	239	71% helix, 0% strand	P0AEY3
B	Protein mazg	protein	222	70% helix, 0% strand	P0AEY3

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	200	0.69	0.87	24	empty
2	199	0.68	0.86	25	empty
3	216	0.66	0.84	25	empty
4	257	0.61	0.80	34	empty
5	173	0.53	0.79	26	empty

Interfaces

1 interface between chains.

A–B · 6104 Å² buried · 49 hydrogen bonds · protein-protein

Compared structures

3CRA · Crystal Structure of Escherichia coli MazG, the Regulator of Nutritional Stress Response · the same entry in another collection · chain A against A, TM-score 1.00
P0AEY3 · AlphaFold monomer V2.0 prediction for nucleoside triphosphate pyrophosphohydrolase… · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P0AEY3
Elsewhere: RCSB PDB 3CRA · PDBe 3CRA · UniProt P0AEY3

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