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Reduced phosphoribulokinase from Synechococcus elongatus PCC 7942 complexed with adenosine diphosphate and glucose 6-phosphate
Analyse Reduced phosphoribulokinase from Synechococcus elongatus PCC 7942 complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KEV
- Type
- protein
- Length
- 317 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.50614
- Source
- Synechococcus elongatus (strain PCC 7942)
- Molecule
- Phosphoribulokinase
- EC
- 2.7.1.19
- UniProt
- Q31PL2
- Ligands
- ADP, G6P
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · resolution 2.50614 · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribulokinase (EC 2.7.1.19) | protein | 317 | 35% helix, 26% strand | Q31PL2 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · chains A
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.49 | 0.83 | 20 | ADP |
| 2 | 144 | 0.44 | 0.75 | 32 | G6P |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6KEV · Reduced phosphoribulokinase from synechococcus elongatus pcc 7942 complexed with… · 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 Q31PL2
- Elsewhere: RCSB PDB 6KEV · PDBe 6KEV · UniProt Q31PL2
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