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The crystal structure of the apo form of mtb mazf

Analyse The crystal structure of the apo form of mtb mazf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WYG
Type: protein
Length: 211 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable endoribonuclease MAZF7
EC: 3.1.-.-
UniProt: P0CL62
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable endoribonuclease MAZF7 (EC 3.1.-.-)	protein	105	25% helix, 36% strand	P0CL62
C	Probable endoribonuclease MAZF7 (EC 3.1.-.-)	protein	106	25% helix, 36% strand	P0CL62

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.37	0.77	17	empty
2	59	0.28	0.74	12	empty

Interfaces

1 interface between chains.

A–C · 1022 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

5WYG · The crystal structure of the apo form of Mtb MazF · the same entry in another collection · chain A against A, TM-score 1.00
P0CL62 · AlphaFold monomer V2.0 prediction for probable endoribonuclease MAZF7 (P0CL62) · a predicted model of the same protein · chain C against A, TM-score 0.98

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 P0CL62
Elsewhere: RCSB PDB 5WYG · PDBe 5WYG · UniProt P0CL62

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