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Crystal structure of a metallochaperone with a tetranuclear CU(I) cluster

Analyse Crystal structure of a metallochaperone with a tetranuclear CU(I) cluster in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QIF
Type: protein
Length: 137 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Copper chaperone copz
UniProt: O32221
Ligands: CU1, CA

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Copper chaperone copz	protein	69	32% helix, 33% strand	O32221
B	Copper chaperone copz	protein	68	32% helix, 34% strand	O32221

Ligands and binding sites

CU1 · Copper (I) ion · metal · 4 copies · chains A, B
CA · Calcium ion · metal · chains B
ACT · Acetate ion · additive · 2 copies · chains A
GOL · Glycerol · additive · chains A

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

Interfaces

1 interface between chains.

A–B · 214 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2QIF · Crystal structure of a metallochaperone with a tetranuclear Cu(I) cluster · the same entry in another collection · chain A against A, TM-score 1.00
O32221 · AlphaFold monomer V2.0 prediction for copper chaperone copz (O32221) · a predicted model of the same protein · chain B 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 O32221
Elsewhere: RCSB PDB 2QIF · PDBe 2QIF · UniProt O32221

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