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Crystal structure of the mouse pd-1 and pd-L2 complex

Analyse Crystal structure of the mouse pd-1 and pd-L2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3BP5
Type
protein
Length
305 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Programmed cell death protein 1; Programmed cell death 1 ligand 2
UniProt
Q02242, Q9WUL5

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProgrammed cell death protein 1protein1143% helix, 54% strandQ02242
BProgrammed cell death 1 ligand 2protein1918% helix, 55% strandQ9WUL5

Ligands and binding sites

  • GOL · Glycerol · additive · chains A, B

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

Interfaces

1 interface between chains.

  • A–B · 1010 Ų buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 3BP5 · Crystal structure of the mouse PD-1 and PD-L2 complex · the same entry in another collection · chain A against A, 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 0.98
  • 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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