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Crystal structure of the RPA2492 protein in complex with SAM from Rhodopseudomonas palustris, Northeast Structural Genomics Consortium Target RpR299

Analyse Crystal structure of the RPA2492 protein in complex with SAM from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3E23
Type: protein
Length: 198 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.6
Source: Rhodopseudomonas palustris
Molecule: uncharacterized protein RPA2492
UniProt: Q6N6X2
Ligands: SAM, SO4
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · resolution 1.6 · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	uncharacterized protein RPA2492	protein	198	35% helix, 27% strand	Q6N6X2

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
SO4 · Sulfate ion · ion · 5 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	305	0.80	0.91	47	SO4, SAM

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

3E23 · Crystal structure of the RPA2492 protein in complex with SAM from rhodopseudomonas… · 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 Q6N6X2
Elsewhere: RCSB PDB 3E23 · PDBe 3E23 · UniProt Q6N6X2

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