Research workbench
Crystal structure of a putative DNA replication regulator hda (SAMA_1916) from shewanella amazonensis SB2B at 3.00 a resolution
Analyse Crystal structure of a putative DNA replication regulator hda (SAMA_1916) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SC3
- Type
- protein
- Length
- 423 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative DNA replication regulator hda
- UniProt
- A1S6W5
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative DNA replication regulator hda | protein | 212 | 51% helix, 12% strand | A1S6W5 |
| B | Putative DNA replication regulator hda | protein | 211 | 52% helix, 11% strand | A1S6W5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.45 | 0.74 | 24 | empty |
| 2 | 142 | 0.42 | 0.75 | 18 | empty |
| 3 | 61 | 0.41 | 0.81 | 14 | empty |
| 4 | 68 | 0.29 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1187 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 3SC3 · Crystal structure of a Putative DNA replication regulator Hda (Sama_1916) from SHEWANELLA… · 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 A1S6W5
- Elsewhere: RCSB PDB 3SC3 · PDBe 3SC3 · UniProt A1S6W5
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