MolNFT v1 · #49624 · protein
Structure of SEC23-SAR1 complexed with the active fragment of SEC31
2QTV: “Structure of SEC23-SAR1 complexed with the active fragment of SEC31”. X-ray diffraction. MolNFT v1 #49624 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2QTV
- Type
- protein
- Length
- 933 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15303, P20606, P38968
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 733 | — | P15303 |
| B | — | protein | 164 | — | P20606 |
| D | — | protein | 36 | — | P38968 |
Compared structures
- 2QTV · Structure of Sec23-Sar1 complexed with the active fragment of Sec31 · the same entry in another collection · chain A against A, TM-score 1.00
- P15303 · AlphaFold monomer V2.0 prediction for protein transport protein SEC23 (P15303) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P20606 · AlphaFold monomer V2.0 prediction for small copii coat GTPase SAR1 (P20606) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P38968 · AlphaFold monomer V2.0 prediction for protein transport protein SEC31 (P38968) · a predicted model of the same protein · chain D against A, TM-score 0.32
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 P15303
- Every structure of UniProt P20606
- Every structure of UniProt P38968
- Elsewhere: RCSB PDB 2QTV · PDBe 2QTV · UniProt P15303 · UniProt P20606 · UniProt P38968
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.