Research workbench
Structure of synechocystis PCC6803 ccmr regulatory domain in complex with 2-pg
Analyse Structure of synechocystis PCC6803 ccmr regulatory domain in complex with 2-pg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y2W
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rubisco operon transcriptional regulator
- UniProt
- P73862
- Ligands
- PGA
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rubisco operon transcriptional regulator | protein | 208 | 32% helix, 28% strand | P73862 |
Ligands and binding sites
- PGA · 2-phosphoglycolic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.33 | 0.74 | 16 | empty |
Compared structures
- 5Y2W · Structure of Synechocystis PCC6803 CcmR regulatory domain in complex with 2-PG · 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 P73862
- Elsewhere: RCSB PDB 5Y2W · PDBe 5Y2W · UniProt P73862
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