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Structural basis of N-end rule substrate recognition in escherichia COLI by the clpap adaptor protein clps - the phe peptide structure

Analyse Structural basis of N-end rule substrate recognition in escherichia COLI by the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WA8
Type
protein
Length
207 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent clp protease adapter protein clps; N-end rule peptide
UniProt
P0A8Q6

Structure

x-ray diffraction · 4 distinct chains · 44% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AATP-dependent clp protease adapter protein clpsprotein8849% helix, 25% strandP0A8Q6
BN-end rule peptideprotein100% helix, 10% strand—
CATP-dependent clp protease adapter protein clpsprotein10347% helix, 21% strandP0A8Q6
DN-end rule peptideprotein60% helix, 17% strand—

Interfaces

2 interfaces between chains.

  • A–B · 522 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 351 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 2WA8 · Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A8Q6 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease adapter protein clps… · a predicted model of the same protein · chain A against A, TM-score 0.96

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