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Crystal structure of the PEPTIDE(PRO)9 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)9 bound complex of N-terminal domain and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BTB
Type: protein
Length: 240 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.899
Source: HOMO SAPIENS; SYNTHETIC CONSTRUCT
Molecule: Prolyl 4-hydroxylase subunit alpha-1; Poly proline peptide
EC: 1.14.11.2
UniProt: P13674

Structure

x-ray diffraction · resolution 1.899 · 2 distinct chains · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prolyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2)	protein	231	77% helix, 0% strand	P13674
C	Poly proline peptide	protein	9	0% helix, 0% strand	—

Interfaces

1 interface between chains.

A–C · 494 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4BTB · Crystal structure of the PEPTIDE(PRO)9 bound complex of N-terminal domain and peptide… · 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 0.90

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P13674
Elsewhere: RCSB PDB 4BTB · PDBe 4BTB · UniProt P13674

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