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Crystal structure of the apo form of a copper-sensitive operon regulator (csor) protein from streptomyces lividans

Analyse Crystal structure of the apo form of a copper-sensitive operon regulator (csor)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ADZ
Type
protein
Length
180 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Csor
UniProt
D6EK73
Ligands
SO4

Structure

x-ray diffraction · 1 distinct chain · 91% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCsorprotein9091% helix, 0% strandD6EK73

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 6 copies · chains A, B

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

Interfaces

1 interface between chains.

  • A–B · 1072 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 4ADZ · Crystal Structure of the apo form of a Copper-sensitive operon Regulator (CsoR) protein… · the same entry in another collection · chain A against A, TM-score 1.00

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