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Modified single helix from the B-domain of protein a bound to IGG1 Fc

Analyse Modified single helix from the B-domain of protein a bound to IGG1 Fc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5U66
Type: protein
Length: 221 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Stapled peptide from domain B of protein a; IGG1 Fc derived from CD4-Fc fusion
UniProt: Q6MZV7
Ligands: NAG, MAN, BMA, GAL

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Stapled peptide from domain B of protein a	protein	14	64% helix, 0% strand	—
A	IGG1 Fc derived from CD4-Fc fusion	protein	207	11% helix, 49% strand	Q6MZV7

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
BMA · beta-D-mannopyranose · sugar · chains A
GAL · beta-D-galactopyranose · sugar · chains A
SIN · Succinic acid · additive · chains B, A

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

Interfaces

1 interface between chains.

B–A · 564 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide, 2 modified, 1 covalent, 1 glycan (disulfide, nonstandard, additive adduct, N-glycosylation).

Compared structures

5U66 · Modified single helix from the B-domain of protein A bound to IgG1 Fc · the same entry in another collection · chain B against B, 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
Every structure of UniProt Q6MZV7
Elsewhere: RCSB PDB 5U66 · PDBe 5U66 · UniProt Q6MZV7

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