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The crystal structure of maf protein of bacillus subtilis

Analyse The crystal structure of maf protein of bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HEB
Type: protein
Length: 365 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Septum formation protein maf
UniProt: Q02169
Ligands: UNX
Pockets: 4 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Septum formation protein maf	protein	182	36% helix, 27% strand	Q02169
B	Septum formation protein maf	protein	183	39% helix, 27% strand	Q02169

Ligands and binding sites

UNX · Unknown atom or ion · ion · 31 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	199	0.54	0.79	33	UNX
2	151	0.48	0.78	31	UNX
3	76	0.42	0.79	17	empty
4	68	0.36	0.77	12	empty

Interfaces

1 interface between chains.

A–B · 1176 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4HEB · The Crystal structure of Maf protein of Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
Q02169 · AlphaFold monomer V2.0 prediction for DTTP/UTP pyrophosphatase (Q02169) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q02169
Elsewhere: RCSB PDB 4HEB · PDBe 4HEB · UniProt Q02169

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