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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 1-244) 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
4BTA
Type
protein
Length
457 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.95
Source
HOMO SAPIENS
Molecule
Prolyl 4-hydroxylase subunit alpha-1; Proline rich peptide
EC
1.14.11.2
UniProt
P13674
Pockets
7 · best druggability 0.47

Structure

x-ray diffraction · resolution 2.95 · 3 distinct chains · 80% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProlyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2)protein23780% helix, 0% strandP13674
BProlyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2)protein21183% helix, 0% strandP13674
CProline rich peptideprotein90% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12070.470.7425empty
2900.420.7813empty
3570.410.8218empty
41050.390.7520empty
51040.340.7320empty

Interfaces

2 interfaces between chains.

  • A–B · 3498 Ų buried · 33 hydrogen bonds · protein-protein
  • A–C · 452 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 4BTA · 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 0.96

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