MolNFT v1 · #125100 · protein
Crystal structure of SEC23 and TANGO1 PEPTIDE3 complex
5KYW: “Crystal structure of SEC23 and TANGO1 PEPTIDE3 complex”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #125100 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5KYW
- Type
- protein
- Length
- 1,483 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15436, O94855
- Ligands
- ZN
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 714 | — | Q15436 |
| B | — | protein | 766 | — | O94855 |
| C | — | protein | 3 | — | — |
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.
Compared structures
- 5KYW · crystal structure of Sec23 and TANGO1 peptide3 complex · the same entry in another collection · chain A against A, TM-score 1.00
- O94855 · AlphaFold monomer V2.0 prediction for protein transport protein SEC24D (O94855) · a predicted model of the same protein · chain B against A, TM-score 1.00
- Q15436 · AlphaFold monomer V2.0 prediction for protein transport protein SEC23A (Q15436) · a predicted model of the same protein · chain A against A, TM-score 0.99
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
- Every structure of UniProt O94855
- Elsewhere: RCSB PDB 5KYW · PDBe 5KYW · UniProt Q15436 · UniProt O94855
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.