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Crystal structure of E-R clpx hexamer

Analyse Crystal structure of E-R clpx hexamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4I63
Type: protein
Length: 1,846 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P0A6H1

Structure

x-ray diffraction · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	311	—	P0A6H1
B	—	protein	307	—	P0A6H1
C	—	protein	298	—	P0A6H1
D	—	protein	310	—	P0A6H1
E	—	protein	315	—	P0A6H1
F	—	protein	305	—	P0A6H1

Compared structures

4I63 · Crystal Structure of E-R ClpX Hexamer · the same entry in another collection · chain F against F, TM-score 1.00
P0A6H1 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit… · a predicted model of the same protein · chain E against A, TM-score 0.95

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P0A6H1
Elsewhere: RCSB PDB 4I63 · PDBe 4I63 · UniProt P0A6H1

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