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Resting state of the E. COLI MRE11-RAD50 (sbccd) head complex bound to atpgs

Analyse Resting state of the E. COLI MRE11-RAD50 (sbccd) head complex bound to atpgs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6S6V
Type
protein
Length
1,498 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
C3TMC7, A0A037YDI0
Ligands
AGS, MN, MG

Structure

electron microscopy · 4 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein386—C3TMC7
B—protein385—C3TMC7
C—protein364—A0A037YDI0
D—protein363—A0A037YDI0

Ligands and binding sites

  • AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 2 copies · chains C, D
  • MN · Manganese (II) ion · metal · 4 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 6S6V · Resting state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ATPgS · the same entry in another collection · chain A against A, TM-score 1.00

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