Research workbench
AlphaFold monomer V2.0 prediction for prolyl 4-hydroxylase subunit alpha-2 (O15460)
Analyse AlphaFold monomer V2.0 prediction for prolyl 4-hydroxylase subunit alpha-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O15460
- Type
- protein
- Length
- 535 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- Prolyl 4-hydroxylase subunit alpha-2
- UniProt
- O15460
- Pockets
- 8 · best druggability 0.72
Structure
1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl 4-hydroxylase subunit alpha-2 | protein | 535 | 47% helix, 14% strand | O15460 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.72 | 0.82 | 52 | empty |
| 2 | 295 | 0.59 | 0.78 | 34 | empty |
| 3 | 407 | 0.58 | 0.74 | 37 | empty |
| 4 | 222 | 0.49 | 0.75 | 29 | empty |
| 5 | 106 | 0.40 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7ZSC · Crystal structure of the heterodimeric human C-P4H-II with truncated alpha subunit… · an experimental structure of the same protein · chain A against A, TM-score 0.43
- 6EVM · Crystal structure of a Pro-9 complexed peptide-substrate-binding domain of human type II… · an experimental structure of the same protein · chain A against A, TM-score 0.18
- 6EVM · Crystal structure of a pro-9 complexed peptide-substrate-binding domain of human type II… · an experimental structure of the same protein · chain A against A, TM-score 0.18
- 6EVL · Crystal structure of an unlignaded peptide-substrate-binding domain of human type II… · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6EVL · Crystal structure of an unlignaded peptide-substrate-binding domain of human type II… · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6EVO · Crystal structure the peptide-substrate-binding domain of human type II collagen prolyl… · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6EVO · Crystal structure the peptide-substrate-binding domain of human type II collagen prolyl… · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6EVN · Crystal structure of peptide-substrate-binding domain of human type II collagen prolyl… · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6EVN · Crystal structure of peptide-substrate-binding domain of human type II collagen prolyl… · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6EVP · Crystal structure the peptide-substrate-binding domain of human type II collagen prolyl… · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6EVP · Crystal structure the peptide-substrate-binding domain of human type II collagen prolyl… · an experimental structure of the same protein · chain A against A, TM-score 0.17
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 O15460
- Elsewhere: UniProt O15460 · AlphaFold DB O15460
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