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Crystal structure of nika from brucella suis in complex with FE(III)- edta

Analyse Crystal structure of nika from brucella suis in complex with FE(III)- edta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OES
Type: protein
Length: 498 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nika protein
UniProt: Q9AL82
Ligands: EDT, FE, SO4
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nika protein	protein	498	32% helix, 22% strand	Q9AL82

Ligands and binding sites

EDT · {[-(bis-carboxymethyl-amino)-ethyl]-carboxymethyl-amino}-acetic acid · ligand · chains A
FE · Fe (III) ion · metal · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
GOL · Glycerol · additive · 3 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	887	0.72	0.76	68	EDT, FE, SO4, GOL
2	134	0.61	0.85	25	empty
3	120	0.55	0.83	26	empty
4	62	0.33	0.76	18	empty

Compared structures

4OES · Crystal structure of NikA from Brucella suis in complex with Fe(III)-EDTA · 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 Q9AL82
Elsewhere: RCSB PDB 4OES · PDBe 4OES · UniProt Q9AL82

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