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MolNFT v1 · #46451 · protein

An arginine ladder in oprp mediates phosphate specific transfer across the outer membrane

2O4V · Porin P: “An arginine ladder in oprp mediates phosphate specific transfer across the outer membrane”. X-ray diffraction, 3 ligands (CA, PO4, CL), 10 pockets (best druggability 0.82). MolNFT v1 #46451 on GenesisL1: 3D structure…

PDB
2O4V
Type
protein
Length
1,233 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Porin P
UniProt
P05695
Ligands
CA, PO4, CL
Pockets
10 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CPorin Pprotein4115% helix, 56% strandP05695

Ligands and binding sites

  • CA · Calcium ion · metal · 3 copies · chains A, B, C
  • PO4 · Phosphate ion · ion · 3 copies · chains A, B, C
  • CL · Chloride ion · ion · chains A, B, C
  • C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 4 copies · chains A, B, C
  • GOL · Glycerol · additive · 2 copies · chains A, C

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

Pockets

10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19570.820.8394PO4
211890.800.82113PO4, GOL
311960.790.81120PO4, GOL
4620.750.9917CL
52210.560.7828C8E

Interfaces

3 interfaces between chains.

  • A–B · 2076 Ų buried · 40 hydrogen bonds · protein-protein
  • A–C · 2067 Ų buried · 39 hydrogen bonds · protein-protein
  • B–C · 2060 Ų buried · 38 hydrogen bonds · protein-protein

Compared structures

  • 2O4V · An arginine ladder in OprP mediates phosphate specific transfer across the outer membrane · the same entry in another collection · chain B against B, TM-score 1.00
  • P05695 · AlphaFold monomer V2.0 prediction for porin P (P05695) · a predicted model of the same protein · chain A against A, TM-score 1.00

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