Research workbench
Crystal structure of the soluble domain of membrane protein implicated in regulation of membrane protease activity from corynebacterium glutamicum
Analyse Crystal structure of the soluble domain of membrane protein implicated in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CP0
- Type
- protein
- Length
- 63 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane protein implicated in regulation of membrane protease activity
- UniProt
- Q6M555
- Ligands
- ZN, CL
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane protein implicated in regulation of membrane protease activity | protein | 63 | 6% helix, 52% strand | Q6M555 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 3CP0 · Crystal structure of the soluble domain of membrane protein implicated in regulation of… · 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 Q6M555
- Elsewhere: RCSB PDB 3CP0 · PDBe 3CP0 · UniProt Q6M555
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.