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Structure of the sbp fpvc in complex with NI2+ ion from P.AERUGINOSA from P21 space group

Analyse Structure of the sbp fpvc in complex with NI2+ ion from P.AERUGINOSA from P21… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6R44
Type: protein
Length: 539 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable adhesion protein
UniProt: Q9I174
Ligands: NI
Pockets: 4 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable adhesion protein	protein	270	45% helix, 11% strand	Q9I174
B	Probable adhesion protein	protein	269	45% helix, 11% strand	Q9I174

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A, B

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

Pockets

4 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	57	0.38	0.80	16	empty
2	63	0.36	0.78	15	empty
3	86	0.34	0.75	18	empty
4	76	0.33	0.75	17	empty

Compared structures

6R44 · Structure of the SBP FpvC in complex with Ni2+ ion from P.aeruginosa from P21 space group · 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 Q9I174
Elsewhere: RCSB PDB 6R44 · PDBe 6R44 · UniProt Q9I174

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