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Crystal structure of a hypothetical protein from neisseria gonorrhoeae with bound ppgpp

Analyse Crystal structure of a hypothetical protein from neisseria gonorrhoeae with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VOG
Type: protein
Length: 176 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative phosphoribosyltransferase
UniProt: A0A1D3HIA2
Ligands: G4P, MG
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative phosphoribosyltransferase	protein	176	30% helix, 34% strand	A0A1D3HIA2

Ligands and binding sites

G4P · Guanosine-5',3'-tetraphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	164	0.48	0.77	28	EDO, G4P, MG

Compared structures

5VOG · Crystal Structure of a Hypothetical Protein from Neisseria gonorrhoeae with bound ppGpp · the same entry in another collection · chain A against A, 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 A0A1D3HIA2
Elsewhere: RCSB PDB 5VOG · PDBe 5VOG · UniProt A0A1D3HIA2

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