MolNFT v1 · #100510 · protein

Mazf from S. aureus crystal form III, C2221, 2.7 a

4MZP · Mazf mRNA interferase: “Mazf from S. aureus crystal form III, C2221, 2.7 a”. X-ray diffraction, 6 pockets (best druggability 0.79). MolNFT v1 #100510 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4MZP
Type: protein
Length: 906 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mazf mRNA interferase
EC: 3.1.-.-
UniProt: Q7A4G9
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 21% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, F, H	Mazf mRNA interferase (EC 3.1.-.-)	protein	114	20% helix, 39% strand	Q7A4G9
B	Mazf mRNA interferase (EC 3.1.-.-)	protein	115	21% helix, 38% strand	Q7A4G9
C, D, G	Mazf mRNA interferase (EC 3.1.-.-)	protein	113	21% helix, 39% strand	Q7A4G9
E	Mazf mRNA interferase (EC 3.1.-.-)	protein	110	22% helix, 40% strand	Q7A4G9

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	918	0.79	0.82	103	empty
2	1096	0.78	0.80	106	empty
3	753	0.78	0.82	88	empty
4	82	0.38	0.77	16	empty
5	62	0.33	0.77	14	empty

Interfaces

17 interfaces between chains.

E–F · 1331 Å² buried · 30 hydrogen bonds · protein-protein
G–H · 1329 Å² buried · 32 hydrogen bonds · protein-protein
A–B · 1316 Å² buried · 32 hydrogen bonds · protein-protein
C–D · 1303 Å² buried · 32 hydrogen bonds · protein-protein
D–F · 298 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4MZP · MazF from S. aureus crystal form III, C2221, 2.7 A · the same entry in another collection · chain H against H, TM-score 1.00
Q7A4G9 · AlphaFold monomer V2.0 prediction for endoribonuclease mazf (Q7A4G9) · a predicted model of the same protein · chain C against A, TM-score 0.97

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 Q7A4G9
Elsewhere: RCSB PDB 4MZP · PDBe 4MZP · UniProt Q7A4G9

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