GL1X · GenesisL1 explorer

MolNFT v1 · #160035 · protein

Structure of P. aeruginosa ATCC27853 HORMA1

6P8P · Uncharacterized protein: “Structure of P. aeruginosa ATCC27853 HORMA1”. X-ray diffraction, 1 ligand (CA), 5 pockets (best druggability 0.58). MolNFT v1 #160035 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6P8P
Type
protein
Length
522 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized protein
UniProt
A0A0F6RRN7
Ligands
CA
Pockets
5 · best druggability 0.58

Structure

x-ray diffraction · 3 distinct chains · 39% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized proteinprotein13239% helix, 23% strandA0A0F6RRN7
B, CUncharacterized proteinprotein13037% helix, 23% strandA0A0F6RRN7
DUncharacterized proteinprotein13040% helix, 23% strandA0A0F6RRN7

Ligands and binding sites

  • CA · Calcium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13090.580.7738empty
22800.560.7743CA
31500.460.7623empty
41190.390.7430empty
51120.380.7514empty

Interfaces

5 interfaces between chains.

  • C–D · 366 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 279 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 240 Ų buried · 5 hydrogen bonds · protein-protein
  • B–D · 240 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 94 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6P8P · Structure of P. aeruginosa ATCC27853 HORMA1 · the same entry in another collection · chain A against A, TM-score 1.00

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