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Structural studies of rolling circle replication initiation protein from staphylococcus aureus

Analyse Structural studies of rolling circle replication initiation protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CWE
Type
protein
Length
540 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Replication initiation protein, replication initiation protein
EC
5.99.1.2
UniProt
P03065, P19529
Pockets
10 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CReplication initiation protein, replication initiation protein (EC 5.99.1.2)protein27041% helix, 30% strandP03065, P19529

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1670.700.9617empty
23780.610.7742empty
31280.400.7522empty
41240.400.7421empty
5840.370.7617empty

Interfaces

1 interface between chains.

  • A–C · 1428 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 4CWE · Structural studies of rolling circle replication initiation protein from Staphylococcus… · the same entry in another collection · chain A against A, TM-score 1.00
  • P03065 · AlphaFold monomer V2.0 prediction for replication initiation protein (P03065) · a predicted model of the same protein · chain A against A, TM-score 0.98
  • P19529 · AlphaFold monomer V2.0 prediction for replication initiation protein (P19529) · a predicted model of the same protein · chain A against A, TM-score 0.98

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