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Crystal structure of the PEPTIDE(PRO-pro-GLY)3 bound complex of N- terminal domain and peptide substrate binding domain of prolyl-4 hydroxylase (residues 1-238) type I from human

Analyse Crystal structure of the PEPTIDE(PRO-pro-GLY)3 bound complex of N- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4BT9
Type
protein
Length
483 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.9
Source
HOMO SAPIENS; SYNTHETIC CONSTRUCT
Molecule
Prolyl 4-hydroxylase subunit alpha-1; (pro-pro-GLY)3 peptide
EC
1.14.11.2
UniProt
P13674
Pockets
4 · best druggability 0.56

Structure

x-ray diffraction · resolution 1.9 · 3 distinct chains · 76% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProlyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2)protein23678% helix, 0% strandP13674
BProlyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2)protein23878% helix, 0% strandP13674
C(pro-pro-GLY)3 peptideprotein90% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12250.560.7831empty
21820.500.7727empty
3640.430.8218empty
4660.320.7515empty

Interfaces

2 interfaces between chains.

  • A–B · 4125 Ų buried · 41 hydrogen bonds · protein-protein
  • A–C · 460 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 4BT9 · Crystal structure of the PEPTIDE(PRO-pro-GLY)3 bound complex of N- terminal domain and… · the same entry in another collection · chain A against A, TM-score 1.00
  • P13674 · AlphaFold monomer V2.0 prediction for prolyl 4-hydroxylase subunit alpha-1 (P13674) · a predicted model of the same protein · chain A against A, TM-score 0.92

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