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Crystal structure of the replication terminator protein mutant RTP.E39K.R42Q

Analyse Crystal structure of the replication terminator protein mutant RTP.E39K.R42Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2DQR
Type
protein
Length
434 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Replication termination protein
UniProt
P68732
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 4 distinct chains · 59% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReplication termination proteinprotein10760% helix, 7% strandP68732
BReplication termination proteinprotein11257% helix, 11% strandP68732
CReplication termination proteinprotein10658% helix, 12% strandP68732
DReplication termination proteinprotein10961% helix, 12% strandP68732

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12330.500.7522empty

Interfaces

4 interfaces between chains.

  • A–B · 1574 Ų buried · 20 hydrogen bonds · protein-protein
  • C–D · 1531 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 51 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 51 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2DQR · Crystal structure of the replication terminator protein mutant RTP.E39K.R42Q · the same entry in another collection · chain A against A, TM-score 1.00

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