Research workbench
Sdea mart-C domain EE/AA nca complex
Analyse Sdea mart-C domain EE/AA nca complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YSI
- Type
- protein
- Length
- 146 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UBIQUITINATING/DEUBIQUITINATING enzyme sdea
- EC
- 3.4.22.-, 2.3.2.-, 2.4.2.31
- UniProt
- Q6RCR0
- Ligands
- NCA
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UBIQUITINATING/DEUBIQUITINATING enzyme sdea (EC 3.4.22.-, 2.3.2.-, 2.4.2.31) | protein | 146 | 28% helix, 34% strand | Q6RCR0 |
Ligands and binding sites
- NCA · Nicotinamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 5YSI · SdeA mART-C domain EE/AA NCA complex · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6RCR0
- Elsewhere: RCSB PDB 5YSI · PDBe 5YSI · UniProt Q6RCR0
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