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Solution structure of human CU(I)COX17

Analyse Solution structure of human CU(I)COX17 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RNB
Type: protein
Length: 67 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C oxidase copper chaperone
UniProt: Q14061
Ligands: CU1

Structure

solution nmr · 1 distinct chain · 42% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C oxidase copper chaperone	protein	67	42% helix, 0% strand	Q14061

Ligands and binding sites

CU1 · Copper (I) ion · metal · chains A

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

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2RNB · Solution structure of human Cu(I)Cox17 · the same entry in another collection · chain A against A, TM-score 1.00
Q14061 · AlphaFold monomer V2.0 prediction for cytochrome C oxidase copper chaperone (Q14061) · a predicted model of the same protein · chain A against A, TM-score 0.58

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 Q14061
Elsewhere: RCSB PDB 2RNB · PDBe 2RNB · UniProt Q14061

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