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Crystal structure of RAE1 (yacp) from bacillus subtilis

Analyse Crystal structure of RAE1 (yacp) from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MQ8
Type: protein
Length: 348 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein yacp
UniProt: P37574
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Uncharacterized protein yacp	protein	174	53% helix, 13% strand	P37574

Ligands and binding sites

GOL · Glycerol · additive · chains D

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	365	0.74	0.85	52	empty
2	100	0.37	0.75	19	empty
3	52	0.33	0.77	12	GOL
4	69	0.30	0.73	12	empty

Interfaces

1 interface between chains.

A–D · 2163 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

5MQ8 · Crystal structure of Rae1 (YacP) from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
P37574 · AlphaFold monomer V2.0 prediction for uncharacterized protein yacp (P37574) · a predicted model of the same protein · chain A against A, TM-score 0.79

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 P37574
Elsewhere: RCSB PDB 5MQ8 · PDBe 5MQ8 · UniProt P37574

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