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Refined structures at 2 ångströms and 2.2 ångströms of the two forms of the H-protein, a lipoamide-containing protein of the glycine decarboxylase complex

Analyse Refined structures at 2 ångströms and 2.2 ångströms of the two forms of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HTP
Type
protein
Length
131 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
H-protein
EC
1.4.4.2
UniProt
P16048
Ligands
OSS
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AH-protein (EC 1.4.4.2)protein13125% helix, 36% strandP16048

Ligands and binding sites

  • OSS · 6-(hydroxyethyldithio)-8-(aminomethylthio)octanoic acid · ligand · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1570.330.7714OSS

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 1HTP · Refined structures at 2 ångströms and 2.2 ångströms of the two forms of the H-protein, a… · the same entry in another collection · chain A against A, TM-score 1.00
  • P16048 · AlphaFold monomer V2.0 prediction for glycine cleavage system H protein, mitochondrial… · a predicted model of the same protein · chain A against A, TM-score 0.99

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