MolNFT v1 · #136746 · protein
De novo design of novel covalent constrained meso-size peptide scaffolds with unique tertiary structures
5V2O: “De novo design of novel covalent constrained meso-size peptide scaffolds with unique tertiary structures”. X-ray diffraction, 2 ligands (TMM, SO4). MolNFT v1 #136746 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5V2O
- Type
- protein
- Length
- 360 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- TMM, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 60 | — | — |
Ligands and binding sites
- TMM · 1,3,5-benzenetricarboxylic acid · ligand · 6 copies · chains A, B, C, D, E, F
- SO4 · Sulfate ion · ion · 7 copies · chains A, B, E, C, D, F
- 2PE · Nonaethylene glycol · additive · 4 copies · chains A, C, B, D
- GOL · Glycerol · additive · 3 copies · chains C, D, A, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5V2O · De Novo Design of Novel Covalent Constrained Meso-size Peptide Scaffolds with Unique… · 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
- Elsewhere: RCSB PDB 5V2O · PDBe 5V2O
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