Research workbench
Crystal structure of semet B. licheniformis cdps yvmc-blic
Analyse Crystal structure of semet B. licheniformis cdps yvmc-blic in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S7T
- Type
- protein
- Length
- 437 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q65EX3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 214 | — | Q65EX3 |
| B | — | protein | 223 | — | Q65EX3 |
Compared structures
- 3S7T · Crystal structure of SeMet B. licheniformis CDPS YvmC-Blic · the same entry in another collection · chain A against A, TM-score 1.00
- Q65EX3 · AlphaFold monomer V2.0 prediction for CYCLO(L-leucyl-L-leucyl) synthase (Q65EX3) · 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 Q65EX3
- Elsewhere: RCSB PDB 3S7T · PDBe 3S7T · UniProt Q65EX3
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