Research workbench
Crystal structure of the SEC3/SSO2 complex at 2.20 ångström resolution
Analyse Crystal structure of the SEC3/SSO2 complex at 2.20 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M4Y
- Type
- protein
- Length
- 1,056 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39926, P33332
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 177 | — | P39926 |
| B, D | — | protein | 173 | — | P33332 |
| C | — | protein | 181 | — | P39926 |
| E | — | protein | 181 | — | P39926 |
| F | — | protein | 171 | — | P33332 |
Ligands and binding sites
- GOL · Glycerol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5M4Y · Crystal structure of the Sec3/Sso2 complex at 2.20 angstrom resolution · the same entry in another collection · chain D against D, TM-score 1.00
- P33332 · AlphaFold monomer V2.0 prediction for exocyst complex component SEC3 (P33332) · a predicted model of the same protein · chain F against A, TM-score 0.99
- P39926 · AlphaFold monomer V2.0 prediction for protein SSO2 (P39926) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P39926
- Every structure of UniProt P33332
- Elsewhere: RCSB PDB 5M4Y · PDBe 5M4Y · UniProt P39926 · UniProt P33332
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