MolNFT v1 · #55625 · protein
Crystal structure of the semet-labeled N-terminal domain and peptide substrate binding domain of alpha subunit of prolyl-4 hydroxylase type I from human.
2YQ8 · Prolyl 4-hydroxylase subunit alpha-1: “Crystal structure of the semet-labeled N-terminal domain and peptide substrate binding domain of alpha…”. X-ray diffraction, 3 pockets (best druggability 0.51). MolNFT v1 #55625 on GenesisL1…
- PDB
- 2YQ8
- Type
- protein
- Length
- 451 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prolyl 4-hydroxylase subunit alpha-1
- EC
- 1.14.11.2
- UniProt
- P13674
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 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 | 225 | 81% helix, 0% strand | P13674 |
| B | Prolyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2) | protein | 226 | 80% helix, 0% strand | P13674 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.51 | 0.76 | 29 | empty |
| 2 | 210 | 0.49 | 0.75 | 39 | empty |
| 3 | 88 | 0.44 | 0.80 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3579 Ų buried · 46 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2YQ8 · Crystal structure of the SeMet-labeled 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 0.96
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 2YQ8 · PDBe 2YQ8 · UniProt P13674
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