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Rada recombinase from methanococcus maripaludis in complex with amppnp and potassium ions

Analyse Rada recombinase from methanococcus maripaludis in complex with amppnp and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EW9
Type: protein
Length: 314 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA repair and recombination protein rada
UniProt: Q977P5
Ligands: ANP, MG, K
Pockets: 3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA repair and recombination protein rada	protein	314	43% helix, 21% strand	Q977P5

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
K · Potassium ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	207	0.43	0.72	28	empty
2	71	0.34	0.76	15	empty
3	79	0.30	0.73	16	empty

Compared structures

3EW9 · RADA recombinase from METHANOCOCCUS MARIPALUDIS in complex with AMPPNP and potassium ions · 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 Q977P5
Elsewhere: RCSB PDB 3EW9 · PDBe 3EW9 · UniProt Q977P5

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