Research workbench
Complex of TRP_CBS1 and CALMODULIN_NLOBE
Analyse Complex of TRP_CBS1 and CALMODULIN_NLOBE in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CQV
- Type
- protein
- Length
- 195 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C6SUZ2, P19334
- Ligands
- CA
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 77 | — | C6SUZ2 |
| A | — | protein | 80 | — | C6SUZ2 |
| B | — | protein | 38 | — | P19334 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains E, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 C6SUZ2
- Every structure of UniProt P19334
- Elsewhere: RCSB PDB 7CQV · PDBe 7CQV · UniProt C6SUZ2 · UniProt P19334
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