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Crystal structure of ppgpp bound rbga from S. aureus

Analyse Crystal structure of ppgpp bound rbga from S. aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6G14
Type: protein
Length: 566 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribosome biogenesis GTPase a
UniProt: A0A0H2XK72
Ligands: G4P
Pockets: 4 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Ribosome biogenesis GTPase a	protein	285	46% helix, 14% strand	A0A0H2XK72
A	Ribosome biogenesis GTPase a	protein	281	45% helix, 15% strand	A0A0H2XK72

Ligands and binding sites

G4P · Guanosine-5',3'-tetraphosphate · ligand · 2 copies · chains B, A

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	836	0.66	0.74	82	G4P
2	95	0.40	0.77	19	empty
3	61	0.31	0.75	12	empty
4	53	0.27	0.74	13	empty

Interfaces

1 interface between chains.

B–A · 259 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6G14 · Crystal structure of ppGpp bound RbgA from S. aureus · the same entry in another collection · chain B against B, TM-score 1.00

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 A0A0H2XK72
Elsewhere: RCSB PDB 6G14 · PDBe 6G14 · UniProt A0A0H2XK72

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