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MolNFT v1 · #40763 · protein

X-ray structure of the chaperone papd in complex with the pilus terminator subunit paph at 2.3 ångström resolution

2J2Z · Chaperone protein papd: “X-ray structure of the chaperone papd in complex with the pilus terminator subunit paph at 2.3 ångström…”. X-ray diffraction, 2 ligands (CO, SO4), 2 pockets (best druggability 0.45). MolNFT v1 #40763 on…

PDB
2J2Z
Type
protein
Length
366 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperone protein papd; Pap fimbrial minor pilin protein
UniProt
P15319, P07111
Ligands
CO, SO4
Pockets
2 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChaperone protein papdprotein2168% helix, 50% strandP15319
BPap fimbrial minor pilin proteinprotein1503% helix, 39% strandP07111

Ligands and binding sites

  • CO · Cobalt (II) ion · metal · chains B
  • SO4 · Sulfate ion · ion · 11 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11280.450.7721empty
2640.340.7712empty

Interfaces

1 interface between chains.

  • A–B · 1984 Ų buried · 41 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2J2Z · X-Ray Structure of the Chaperone PapD in complex with the Pilus terminator subunit PapH… · the same entry in another collection · chain A against A, TM-score 1.00
  • P15319 · AlphaFold monomer V2.0 prediction for chaperone protein papd (P15319) · a predicted model of the same protein · chain A against A, TM-score 0.99
  • P07111 · AlphaFold monomer V2.0 prediction for pap fimbrial minor pilin protein (P07111) · a predicted model of the same protein · chain B against A, TM-score 0.96

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