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Crystal structure of chromosome partitioning protein (para) in complex with ADP from synechocystis sp. northeast structural genomics consortium target SGR89
Analyse Crystal structure of chromosome partitioning protein (para) in complex with ADP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CWQ
- Type
- protein
- Length
- 403 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Para family chromosome partitioning protein
- UniProt
- Q6YRW8
- Ligands
- ADP
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Para family chromosome partitioning protein | protein | 206 | 45% helix, 18% strand | Q6YRW8 |
| B | Para family chromosome partitioning protein | protein | 197 | 49% helix, 19% strand | Q6YRW8 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
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 | 81 | 0.74 | 0.97 | 27 | empty |
| 2 | 105 | 0.42 | 0.77 | 26 | ADP |
| 3 | 106 | 0.40 | 0.76 | 25 | ADP |
| 4 | 80 | 0.33 | 0.74 | 17 | empty |
| 5 | 54 | 0.32 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1005 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3CWQ · Crystal structure of chromosome partitioning protein (ParA) in complex with ADP from… · 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 Q6YRW8
- Elsewhere: RCSB PDB 3CWQ · PDBe 3CWQ · UniProt Q6YRW8
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