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42F3 PCPB7/H-2LD complex

Analyse 42F3 PCPB7/H-2LD complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MVB
Type
protein
Length
621 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
42F3 alpha vmch; 42F3 beta vmch; H-2 class I histocompatibility antigen, L-D alpha chain…
UniProt
P01897
Pockets
10 · best druggability 0.75

Structure

x-ray diffraction · 4 distinct chains · 14% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C42F3 alpha vmchprotein1993% helix, 43% strand—
D42F3 beta vmchprotein2396% helix, 51% strand—
AH-2 class I histocompatibility antigen, L-D alpha chainprotein17437% helix, 32% strandP01897
BPCPB7protein90% helix, 0% strand—

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19230.750.7882empty
21320.500.8034empty
3680.450.8218empty
41230.420.7622empty
51370.400.7432empty

Interfaces

6 interfaces between chains.

  • C–D · 2252 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 867 Ų buried · 13 hydrogen bonds · protein-protein
  • C–A · 397 Ų buried · 4 hydrogen bonds · protein-protein
  • D–A · 351 Ų buried · 4 hydrogen bonds · protein-protein
  • D–B · 207 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 4MVB · 42F3 pCPB7/H-2Ld Complex · the same entry in another collection · chain C against C, TM-score 1.00
  • P01897 · AlphaFold monomer V2.0 prediction for H-2 class I histocompatibility antigen, L-D alpha… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

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