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Structure and refinement of the oxidized P21 form of uteroglobin at 1.64 ångströms resolution

Analyse Structure and refinement of the oxidized P21 form of uteroglobin at 1.64… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2UTG
Type
protein
Length
140 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uteroglobin
UniProt
P02779
Pockets
1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BUteroglobinprotein7073% helix, 0% strandP02779

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11430.810.9627empty

Interfaces

1 interface between chains.

  • A–B · 1530 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2UTG · Structure and refinement of the oxidized P21 form of uteroglobin at 1.64 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02779 · AlphaFold monomer V2.0 prediction for uteroglobin (P02779) · a predicted model of the same protein · chain A against A, TM-score 0.96

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