Research workbench
Crystal structure of VASH1-svbp in complex with epoy
Analyse Crystal structure of VASH1-svbp in complex with epoy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J7B
- Type
- protein
- Length
- 282 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q7L8A9, Q8N300
- Ligands
- BJL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 249 | — | Q7L8A9 |
| B | — | protein | 33 | — | Q8N300 |
Ligands and binding sites
- BJL · N-[(3R)-4-ethoxy-3-hydroxy-4-oxobutanoyl]-L-tyrosine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6J7B · Crystal structure of VASH1-SVBP in complex with epoY · the same entry in another collection · chain A against A, TM-score 1.00
- Q7L8A9 · AlphaFold monomer V2.0 prediction for tubulinyl-tyr carboxypeptidase 1 (Q7L8A9) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q8N300 · AlphaFold monomer V2.0 prediction for small vasohibin-binding protein (Q8N300) · a predicted model of the same protein · chain B against A, TM-score 0.82
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 Q7L8A9
- Every structure of UniProt Q8N300
- Elsewhere: RCSB PDB 6J7B · PDBe 6J7B · UniProt Q7L8A9 · UniProt Q8N300
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