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Structure of E. COLI clps ring complex

Analyse Structure of E. COLI clps ring complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O2O
Type: protein
Length: 680 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent clp protease adaptor protein clps
UniProt: P0A8Q6

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	ATP-dependent clp protease adaptor protein clps	protein	85	51% helix, 27% strand	P0A8Q6

Interfaces

8 interfaces between chains.

G–H · 333 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 326 Å² buried · 5 hydrogen bonds · protein-protein
A–H · 317 Å² buried · 5 hydrogen bonds · protein-protein
B–C · 304 Å² buried · 5 hydrogen bonds · protein-protein
E–F · 297 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3O2O · Structure of E. coli ClpS ring complex · the same entry in another collection · chain H against H, 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 F against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P0A8Q6
Elsewhere: RCSB PDB 3O2O · PDBe 3O2O · UniProt P0A8Q6

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