MolNFT v2 · #87210 · protein
Crystal structure of the apo form of N-terminal domain and peptide substrate binding domain of prolyl-4 hydroxylase type I from human
4BT8 · Prolyl 4-hydroxylase subunit alpha-1: “Crystal structure of the apo form of N-terminal domain and peptide substrate binding domain of prolyl-4…”. X-ray diffraction at 2.198, 4 pockets (best druggability 0.47). MolNFT v2 #87210 on…
- PDB
- 4BT8
- Type
- protein
- Length
- 455 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.198
- Source
- HOMO SAPIENS
- Molecule
- Prolyl 4-hydroxylase subunit alpha-1
- EC
- 1.14.11.2
- UniProt
- P13674
- Pockets
- 4 · best druggability 0.47
Structure
x-ray diffraction · resolution 2.198 · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2) | protein | 222 | 82% helix, 0% strand | P13674 |
| B | Prolyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2) | protein | 233 | 78% helix, 0% strand | P13674 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.47 | 0.76 | 21 | empty |
| 2 | 72 | 0.44 | 0.82 | 18 | empty |
| 3 | 103 | 0.35 | 0.74 | 19 | empty |
| 4 | 63 | 0.29 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3752 Ų buried · 45 hydrogen bonds · protein-protein
Compared structures
- 4BT8 · Crystal structure of the apo form of N-terminal domain and peptide substrate binding… · 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 B against A, TM-score 0.98
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 4BT8 · PDBe 4BT8 · UniProt P13674
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