Research workbench
L-pipecolic acid-bound L-proline cis-4-hydroxylase
Analyse L-pipecolic acid-bound L-proline cis-4-hydroxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P7X
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-proline cis-4-hydroxylase
- EC
- 1.14.11.-
- UniProt
- Q989T9
- Ligands
- AKG, YCP, CO, SO4
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-proline cis-4-hydroxylase (EC 1.14.11.-) | protein | 286 | 30% helix, 25% strand | Q989T9 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- YCP · (2S)-piperidine-2-carboxylic acid · ligand · chains A
- CO · Cobalt (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.79 | 0.97 | 32 | CO, AKG, YCP |
| 2 | 68 | 0.34 | 0.76 | 14 | empty |
Compared structures
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 Q989T9
- Elsewhere: RCSB PDB 4P7X · PDBe 4P7X · UniProt Q989T9
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