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Crystal structure of the haemophilus influenzae E57A mutant fbpa

Analyse Crystal structure of the haemophilus influenzae E57A mutant fbpa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O6A
Type: protein
Length: 307 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iron-utilization periplasmic protein
UniProt: P35755
Ligands: FE, PO4
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Iron-utilization periplasmic protein	protein	307	47% helix, 18% strand	P35755

Ligands and binding sites

FE · Fe (III) ion · metal · chains A
PO4 · Phosphate ion · ion · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	125	0.56	0.83	29	empty
2	274	0.56	0.77	39	PO4

Compared structures

2O6A · Crystal structure of the Haemophilus influenzae E57A mutant FbpA · the same entry in another collection · chain A against A, TM-score 1.00
P35755 · AlphaFold monomer V2.0 prediction for iron-utilization periplasmic protein (P35755) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P35755
Elsewhere: RCSB PDB 2O6A · PDBe 2O6A · UniProt P35755

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