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Structure of homo-dimeric staphylococcus capitis divalent metal ion transporter (dmt) by nabfab-fiducial assisted cryo-EM

Analyse Structure of homo-dimeric staphylococcus capitis divalent metal ion transporter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7PHQ
Type
protein
Length
2,136 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nabfab hc; Nabfab lc; Divalent metal cation transporter mnth; Dmt-NB16_4; Anti-Fab…
UniProt
A0A4U9TNH6
Pockets
20 · best druggability 0.74

Structure

electron microscopy · 5 distinct chains · 32% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
H, ANabfab hcprotein2219% helix, 44% strand—
L, CNabfab lcprotein2084% helix, 43% strand—
B, DDivalent metal cation transporter mnthprotein39878% helix, 0% strandA0A4U9TNH6
N, EDmt-NB16_4protein1210% helix, 32% strand—
K, FAnti-Fab nanobodyprotein1208% helix, 50% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17900.740.7878empty
27750.730.7878empty
32990.610.7942empty
44300.600.7569empty
53780.580.7554empty

Interfaces

11 interfaces between chains.

  • H–L · 1905 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 1904 Ų buried · 16 hydrogen bonds · protein-protein
  • D–E · 813 Ų buried · 11 hydrogen bonds · protein-protein
  • B–N · 813 Ų buried · 11 hydrogen bonds · protein-protein
  • H–N · 765 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 7PHQ · Structure of homo-dimeric Staphylococcus capitis divalent metal ion transporter (DMT) by… · the same entry in another collection · chain L against L, TM-score 1.00

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