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Crystal structure of staphylococcus aureus sira complexed with staphyloferrin B

Analyse Crystal structure of staphylococcus aureus sira complexed with staphyloferrin B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MWF
Type: protein
Length: 292 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iron-regulated ABC transporter siderophore-binding protein sira
UniProt: Q7A869
Ligands: SE8, FE
Pockets: 1 · best druggability 0.51

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Iron-regulated ABC transporter siderophore-binding protein sira	protein	292	47% helix, 18% strand	Q7A869

Ligands and binding sites

SE8 · 5-[(2-{[(3S)-5-{[(2S)-2-amino-2-carboxyethyl]amino}-3-carboxy-3-hydroxy-5-oxopentanoyl]amino}ethyl)amino]-2,5-dioxopentanoic acid · ligand · chains A
FE · Fe (III) ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	145	0.51	0.79	22	FE, SE8

Compared structures

3MWF · Crystal structure of Staphylococcus aureus SirA complexed with staphyloferrin B · 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 Q7A869
Elsewhere: RCSB PDB 3MWF · PDBe 3MWF · UniProt Q7A869

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