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Ex silico engineering of cystine-dense peptides yielding a potent bispecific T-cell engager

Analyse Ex silico engineering of cystine-dense peptides yielding a potent bispecific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7SJQ
Type: protein
Length: 150 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Programmed cell death 1 ligand 1; Cystine-dense peptide
UniProt: Q9NZQ7
Ligands: NAG, NA, SO4

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Programmed cell death 1 ligand 1	protein	117	14% helix, 50% strand	Q9NZQ7
D	Cystine-dense peptide	protein	33	79% helix, 0% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
NA · Sodium ion · metal · chains A
SO4 · Sulfate ion · ion · 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–D · 587 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

7SJQ · Ex silico engineering of cystine-dense peptides yielding a potent bispecific T-cell… · the same entry in another collection · chain D against D, 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 Q9NZQ7
Elsewhere: RCSB PDB 7SJQ · PDBe 7SJQ · UniProt Q9NZQ7

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