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Crystal structure of an uncharacterized cystatin fold protein (saro_2299) from novosphingobium aromaticivorans dsm at 1.90 A resolution

Analyse Crystal structure of an uncharacterized cystatin fold protein (saro_2299) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FF2
Type
protein
Length
117 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.9
Source
Novosphingobium aromaticivorans DSM 12444
Molecule
uncharacterized cystatin fold protein (YP_497570.1) from NTF2 superfamily
UniProt
Q2G5Y7
Pockets
1 · best druggability 0.54

Structure

x-ray diffraction · resolution 1.9 · 1 distinct chain · 28% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Auncharacterized cystatin fold protein (YP_497570.1) from NTF2 superfamilyprotein11728% helix, 42% strandQ2G5Y7

Ligands and binding sites

  • ACT · Acetate ion · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11040.540.8323ACT

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 3FF2 · Crystal structure of an uncharacterized cystatin fold protein (SARO_2299) from… · the same entry in another collection · chain A against A, TM-score 1.00

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