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Crystal structure of streptococcus pneumoniae TIGR4 piaa in complex with bis-tris propane

Analyse Crystal structure of streptococcus pneumoniae TIGR4 piaa in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HMO
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iron-compound ABC transporter, iron compound-binding protein
UniProt: Q97R09
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Iron-compound ABC transporter, iron compound-binding protein	protein	308	41% helix, 18% strand	Q97R09

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A
B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	288	0.59	0.78	38	GOL, B3P
2	56	0.34	0.77	17	empty
3	66	0.32	0.75	14	empty

Compared structures

4HMO · Crystal structure of streptococcus pneumoniae TIGR4 PiaA in complex with Bis-tris propane · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q97R09
Elsewhere: RCSB PDB 4HMO · PDBe 4HMO · UniProt Q97R09

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