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A novel protein fold forms an intramolecular lock to stabilize the tertiary structure of streptococcus mutans adhesin P1

Analyse A novel protein fold forms an intramolecular lock to stabilize the tertiary… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4TSH
Type
protein
Length
606 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Surface protein adhesin
UniProt
C9E3B4
Ligands
CA, MG
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASurface protein adhesinprotein12155% helix, 14% strandC9E3B4
BSurface protein adhesinprotein48513% helix, 43% strandC9E3B4

Ligands and binding sites

  • CA · Calcium ion · metal · 2 copies · chains B
  • MG · Magnesium ion · metal · 2 copies · chains B, 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1690.360.7817empty

Interfaces

1 interface between chains.

  • A–B · 3309 Ų buried · 60 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 isopeptide (isopeptide).

Compared structures

  • 4TSH · A Novel Protein Fold Forms an Intramolecular Lock to Stabilize the Tertiary Structure of… · the same entry in another collection · chain A against A, TM-score 1.00

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