Research workbench
Crystal structure of human trans-3-hydroxy-L-proline dehydratase
Analyse Crystal structure of human trans-3-hydroxy-L-proline dehydratase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QPO
- Type
- protein
- Length
- 666 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trans-3-hydroxy-L-proline dehydratase
- EC
- 4.2.1.77
- UniProt
- Q96EM0
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-3-hydroxy-L-proline dehydratase (EC 4.2.1.77) | protein | 329 | 19% helix, 37% strand | Q96EM0 |
| B | Trans-3-hydroxy-L-proline dehydratase (EC 4.2.1.77) | protein | 337 | 19% helix, 36% strand | Q96EM0 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 735 | 0.79 | 0.83 | 37 | empty |
| 2 | 119 | 0.76 | 0.95 | 28 | empty |
| 3 | 145 | 0.75 | 0.93 | 30 | empty |
| 4 | 99 | 0.56 | 0.85 | 20 | empty |
| 5 | 89 | 0.52 | 0.84 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2001 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7QPO · Crystal structure of human trans-3-Hydroxy-L-proline dehydratase · the same entry in another collection · chain A against A, TM-score 1.00
- Q96EM0 · AlphaFold monomer V2.0 prediction for trans-3-hydroxy-L-proline dehydratase (Q96EM0) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q96EM0
- Elsewhere: RCSB PDB 7QPO · PDBe 7QPO · UniProt Q96EM0
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