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Crystal structure of staphylococcus capitis divalent metal ion transporter (dmt) in complex with nanobody

Analyse Crystal structure of 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
4WGV
Type
protein
Length
1,030 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Divalent metal cation transporter mnth; Camelid antibody fragment, nanobody
UniProt
F9L8R0
Pockets
20 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CDivalent metal cation transporter mnthprotein39572% helix, 0% strandF9L8R0
B, DCamelid antibody fragment, nanobodyprotein1203% helix, 57% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17460.700.7778empty
2670.680.9526empty
35140.650.7649empty
41360.640.8622empty
53370.610.7841empty

Interfaces

4 interfaces between chains.

  • D–C · 842 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 828 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 610 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 503 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

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