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Crystal structure of peptide-substrate-binding domain of human type I collagen prolyl 4-hydroxylase

Analyse Crystal structure of peptide-substrate-binding domain of human type I collagen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TJC
Type: protein
Length: 190 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prolyl 4-hydroxylase alpha-1 subunit
EC: 1.14.11.2
UniProt: P13674
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Prolyl 4-hydroxylase alpha-1 subunit (EC 1.14.11.2)	protein	95	76% helix, 0% strand	P13674

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	155	0.48	0.77	21	empty

Interfaces

1 interface between chains.

A–B · 532 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1TJC · Crystal structure of peptide-substrate-binding domain of human type I collagen prolyl… · 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 0.97

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 1TJC · PDBe 1TJC · UniProt P13674

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