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Cryo-EM structure of human MCT1 in complex with basigin-2 in the presence of lactate

Analyse Cryo-EM structure of human MCT1 in complex with basigin-2 in the presence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LZ0
Type
protein
Length
591 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Monocarboxylate transporter 1; Basigin
UniProt
P53985, P35613
Ligands
2OP
Pockets
5 · best druggability 0.77

Structure

electron microscopy · 2 distinct chains · 57% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMonocarboxylate transporter 1protein37581% helix, 0% strandP53985
BBasiginprotein21616% helix, 47% strandP35613

Ligands and binding sites

  • 2OP · (2S)-2-hydroxypropanoic acid · ligand · chains A

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16290.770.82642OP
24260.710.8371empty
33080.610.7957empty
4960.430.7920empty
5500.420.8217empty

Interfaces

1 interface between chains.

  • A–B · 727 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6LZ0 · Cryo-EM structure of human MCT1 in complex with Basigin-2 in the presence of lactate · the same entry in another collection · chain A against A, TM-score 1.00
  • P53985 · AlphaFold monomer V2.0 prediction for monocarboxylate transporter 1 (P53985) · a predicted model of the same protein · chain A against A, TM-score 0.79
  • P35613 · AlphaFold monomer V2.0 prediction for basigin (P35613) · a predicted model of the same protein · chain B against A, TM-score 0.73

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