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Coiled coil peptide metal coordination framework: trimer fold

Analyse Coiled coil peptide metal coordination framework: trimer fold in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5U5B
Type: protein
Length: 84 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Designed trimeric coiled coil peptide with two terpyridine side chains
Ligands: ACE, CU, NH2

Structure

x-ray diffraction · 1 distinct chain · 93% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Designed trimeric coiled coil peptide with two terpyridine side chains	protein	28	93% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 3 copies · chains A, B, C
CU · Copper (II) ion · metal · 7 copies · chains A, C, B
NH2 · Amino group · ion · 3 copies · chains A, C, B
GOL · Glycerol · additive · chains A, B

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

Interfaces

3 interfaces between chains.

A–C · 623 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 603 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 553 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified, 3 covalent (nonstandard, covalent ligand).

Compared structures

5U5B · Coiled Coil Peptide Metal Coordination Framework: Trimer Fold · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 5U5B · PDBe 5U5B

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