Research workbench
Aspartyl/Asparaginyl beta-hydroxylase (AspH) H725A in complex with Factor X peptide fragment (39mer-4Ser)
Analyse Aspartyl/Asparaginyl beta-hydroxylase (AspH) H725A in complex with Factor X… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E6J
- Type
- protein
- Length
- 447 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Aspartyl/asparaginyl beta-hydroxylase; Peptide from Factor X light chain
- EC
- 1.14.11.16
- UniProt
- Q12797, P00742
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · resolution 1.9 · 2 distinct chains · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) | protein | 429 | 53% helix, 16% strand | Q12797 |
| B | Peptide from Factor X light chain | protein | 18 | 0% helix, 0% strand | P00742 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.75 | 0.99 | 18 | PPI |
| 2 | 107 | 0.57 | 0.85 | 29 | empty |
| 3 | 107 | 0.44 | 0.78 | 26 | empty |
| 4 | 108 | 0.38 | 0.74 | 28 | empty |
| 5 | 85 | 0.34 | 0.75 | 20 | GOL |
Interfaces
1 interface between chains.
- A–B · 1248 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7E6J · ASPARTYL/ASPARAGINYL beta-hydroxylase (asph) H725A in complex with factor X peptide… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12797 · AlphaFold monomer V2.0 prediction for ASPARTYL/ASPARAGINYL beta- hydroxylase (Q12797) · a predicted model of the same protein · chain A against A, TM-score 1.00
- P00742 · AlphaFold monomer V2.0 prediction for coagulation factor X (P00742) · a predicted model of the same protein · chain B against A, TM-score 0.21
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 Q12797
- Every structure of UniProt P00742
- Elsewhere: RCSB PDB 7E6J · PDBe 7E6J · UniProt Q12797 · UniProt P00742
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