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Designed peptide alpha-1, P1 form

Analyse Designed peptide alpha-1, P1 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BYZ
Type: protein
Length: 48 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (synthetic designed peptide "alpha-1")
Ligands: ACE, ETA, CL

Structure

x-ray diffraction · 1 distinct chain · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Protein (synthetic designed peptide "alpha-1")	protein	12	83% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 4 copies · chains A, B, C, D
ETA · Ethanolamine · ligand · 2 copies · chains A, C
CL · Chloride ion · ion · chains C
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B, C, D
MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A, D

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

Interfaces

4 interfaces between chains.

A–B · 324 Å² buried · 1 hydrogen bond · protein-protein
C–D · 316 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 82 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 54 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 covalent (covalent ligand).

Compared structures

1BYZ · Designed peptide alpha-1, P1 form · 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 1BYZ · PDBe 1BYZ

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