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Crystal structure of the complex between the extracellular domains of mouse pd-1 mutant and pd-L2

Analyse Crystal structure of the complex between the extracellular domains of mouse… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3RNQ
Type
protein
Length
296 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Programmed cell death 1 ligand 2; Programmed cell death protein 1
UniProt
Q9WUL5, Q02242

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BProgrammed cell death 1 ligand 2protein1848% helix, 56% strandQ9WUL5
AProgrammed cell death protein 1protein1123% helix, 55% strandQ02242

Interfaces

1 interface between chains.

  • B–A · 955 Ų buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 3RNQ · Crystal structure of the complex between the extracellular domains of mouse PD-1 mutant… · the same entry in another collection · chain B against B, TM-score 1.00
  • Q02242 · AlphaFold monomer V2.0 prediction for programmed cell death protein 1 (Q02242) · a predicted model of the same protein · chain A against A, TM-score 0.97
  • Q9WUL5 · AlphaFold monomer V2.0 prediction for programmed cell death 1 ligand 2 (Q9WUL5) · a predicted model of the same protein · chain B against A, TM-score 0.96

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