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1.65 ångström crystal structure of serine-rich repeat adhesion glycoprotein (SRR1) from streptococcus agalactiae

Analyse 1.65 ångström crystal structure of serine-rich repeat adhesion glycoprotein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MBO
Type
protein
Length
308 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serine-rich repeat adhesion glycoprotein (SRR1)
UniProt
Q8E473
Ligands
CA
Pockets
2 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerine-rich repeat adhesion glycoprotein (SRR1)protein3084% helix, 49% strandQ8E473

Ligands and binding sites

  • CA · Calcium ion · metal · 4 copies · chains A
  • BME · Beta-mercaptoethanol · additive · chains A
  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11630.470.7629empty
2580.280.7414empty

Modifications

Observed in the structure: 1 covalent, 1 modified (additive adduct, methylation).

Compared structures

  • 4MBO · 1.65 Angstrom Crystal Structure of Serine-rich Repeat Adhesion Glycoprotein (Srr1) from… · the same entry in another collection · chain A against A, TM-score 1.00

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