MolNFT v1 · #125095 · protein
Structure of SEC23 and TANGO1 complex
5KYN · Protein transport protein SEC23A: “Structure of SEC23 and TANGO1 complex”. X-ray diffraction, 1 ligand (ZN), 20 pockets (best druggability 0.70). MolNFT v1 #125095 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5KYN
- Type
- protein
- Length
- 1,452 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein transport protein SEC23A; Melanoma inhibitory activity protein 3
- UniProt
- Q15436
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein transport protein SEC23A | protein | 730 | 32% helix, 22% strand | Q15436 |
| B | Protein transport protein SEC23A | protein | 719 | 34% helix, 22% strand | Q15436 |
| C | Melanoma inhibitory activity protein 3 | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 500 | 0.70 | 0.80 | 63 | empty |
| 2 | 206 | 0.70 | 0.87 | 30 | empty |
| 3 | 348 | 0.69 | 0.82 | 47 | empty |
| 4 | 232 | 0.67 | 0.84 | 33 | empty |
| 5 | 398 | 0.65 | 0.79 | 57 | empty |
Interfaces
1 interface between chains.
- B–C · 210 Ų buried · 0 hydrogen bonds · protein-protein
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 Q15436
- Elsewhere: RCSB PDB 5KYN · PDBe 5KYN · UniProt Q15436
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