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Crystal structure of putative DNA processing protein DprA from Rhodopseudomonas palustris CGA009

Analyse Crystal structure of putative DNA processing protein DprA from Rhodopseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MAJ
Type: protein
Length: 353 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.05
Source: Rhodopseudomonas palustris
Molecule: DNA processing chain A
UniProt: Q6N563
Ligands: SO4
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · resolution 2.05 · 1 distinct chain · 47% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA processing chain A	protein	353	47% helix, 11% strand	Q6N563

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.61	0.91	20	empty
2	275	0.61	0.80	39	empty
3	140	0.55	0.82	31	empty
4	68	0.45	0.82	18	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

3MAJ · Crystal structure of putative DNA processing protein dpra from rhodopseudomonas palustris… · 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 Q6N563
Elsewhere: RCSB PDB 3MAJ · PDBe 3MAJ · UniProt Q6N563

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