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Crystal structure of the siderophore receptor piua from acinetobacter baumannii

Analyse Crystal structure of the siderophore receptor piua from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FP1
Type: protein
Length: 701 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tonb-dependent siderophore receptor
UniProt: D0CAH3
Ligands: PO4
Pockets: 6 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tonb-dependent siderophore receptor	protein	701	5% helix, 59% strand	D0CAH3

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 8 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	505	0.87	0.93	69	empty
2	126	0.79	0.97	41	empty
3	167	0.78	0.94	39	empty
4	760	0.78	0.82	91	empty
5	1059	0.77	0.79	89	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

5FP1 · Crystal structure of the siderophore receptor PiuA from Acinetobacter baumannii · 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 D0CAH3
Elsewhere: RCSB PDB 5FP1 · PDBe 5FP1 · UniProt D0CAH3

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