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Structure of multidrug and toxin compound extrusion (mate) transporter norm by nabfab-fiducial assisted cryo-EM

Analyse Structure of multidrug and toxin compound extrusion (mate) transporter norm by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7PHP
Type
protein
Length
1,134 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Multidrug resistance protein norm; Nabfab hc; Nabfab lc; Norm-NB17_4; Anti-Fab nanobody
UniProt
D7H904
Pockets
9 · best druggability 0.85

Structure

electron microscopy · 5 distinct chains · 35% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMultidrug resistance protein normprotein45678% helix, 0% strandD7H904
HNabfab hcprotein2288% helix, 44% strand—
LNabfab lcprotein2086% helix, 48% strand—
NNorm-NB17_4protein1222% helix, 40% strand—
KAnti-Fab nanobodyprotein1205% helix, 43% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19290.850.8691empty
2530.680.9715empty
31100.650.8930empty
42090.460.7445empty
5760.370.7719empty

Interfaces

5 interfaces between chains.

  • H–L · 1912 Ų buried · 13 hydrogen bonds · protein-protein
  • A–N · 900 Ų buried · 4 hydrogen bonds · protein-protein
  • H–N · 768 Ų buried · 6 hydrogen bonds · protein-protein
  • L–K · 717 Ų buried · 5 hydrogen bonds · protein-protein
  • L–N · 279 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 7PHP · Structure of Multidrug and Toxin Compound Extrusion (MATE) transporter NorM by… · the same entry in another collection · chain A against A, TM-score 1.00

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