MolNFT v1 · #151840 · protein
Crystal structure of redox-inhibited phosphoribulokinase from synechococcus sp. (strain pcc 6301), osmate derivative
6HZL: “Crystal structure of redox-inhibited phosphoribulokinase from synechococcus sp. (strain pcc 6301), osmate…”. X-ray diffraction, 1 ligand (OS), 5 pockets (best druggability 0.67). MolNFT v1 #151840 on GenesisL1: 3D structure, binding…
- PDB
- 6HZL
- Type
- protein
- Length
- 624 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribulokinase
- EC
- 2.7.1.19
- UniProt
- A0A0H3K6J7
- Ligands
- OS
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribulokinase (EC 2.7.1.19) | protein | 329 | 36% helix, 28% strand | A0A0H3K6J7 |
| B | Phosphoribulokinase (EC 2.7.1.19) | protein | 295 | 32% helix, 31% strand | A0A0H3K6J7 |
Ligands and binding sites
- OS · Osmium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 410 | 0.67 | 0.79 | 51 | OS |
| 2 | 116 | 0.43 | 0.77 | 19 | empty |
| 3 | 103 | 0.41 | 0.77 | 18 | empty |
| 4 | 68 | 0.30 | 0.74 | 21 | empty |
| 5 | 69 | 0.29 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 936 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6HZL · Crystal structure of redox-inhibited phosphoribulokinase from Synechococcus sp. (strain… · 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 A0A0H3K6J7
- Elsewhere: RCSB PDB 6HZL · PDBe 6HZL · UniProt A0A0H3K6J7
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