Crystal structure of the fourth and fifth fibronectin F1 modules in complex with a fragment of staphylococcus aureus fnbpa-1

Structure

x-ray diffraction · 4 distinct chains · 0% helix, 60% strand (DSSP).

Ligands and binding sites

• K · Potassium ion · metal · chains C
• SCN · Thiocyanate ion · ion · 5 copies · chains A, C, D

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.

Interfaces

6 interfaces between chains.

• C–B · 1212 Ų buried · 31 hydrogen bonds · protein-protein
• A–D · 1204 Ų buried · 31 hydrogen bonds · protein-protein
• B–D · 603 Ų buried · 16 hydrogen bonds · protein-protein
• A–C · 481 Ų buried · 14 hydrogen bonds · protein-protein
• A–B · 131 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

• 2RKY · Crystal structure of the fourth and fifth fibronectin F1 modules in complex with a… · the same entry in another collection · chain D against D, TM-score 1.00
• P02751 · AlphaFold monomer V2.0 prediction for fibronectin (P02751) · a predicted model of the same protein · chain C against A, TM-score 0.81
• P14738 · AlphaFold monomer V2.0 prediction for fibronectin-binding protein a (P14738) · a predicted model of the same protein · chain D against A, TM-score 0.25

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 P02751
• Every structure of UniProt P14738
• Elsewhere: RCSB PDB 2RKY · PDBe 2RKY · UniProt P02751 · UniProt P14738