Research workbench
Crystal structure of bacillus stearothermophilus prfa-holliday junction resolvase
Analyse Crystal structure of bacillus stearothermophilus prfa-holliday junction… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FCO
- Type
- protein
- Length
- 308 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Recombination protein U (penicillin-binding protein related factor a)
- EC
- 3.1.22.4
- Ligands
- MG
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Recombination protein U (penicillin-binding protein related factor a) (EC 3.1.22.4) | protein | 154 | 36% helix, 28% strand | — |
| B | Recombination protein U (penicillin-binding protein related factor a) (EC 3.1.22.4) | protein | 154 | 39% helix, 28% strand | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.52 | 0.77 | 32 | empty |
| 2 | 167 | 0.46 | 0.76 | 32 | MG |
| 3 | 56 | 0.27 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 993 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2FCO · Crystal Structure of Bacillus stearothermophilus PrfA-Holliday Junction Resolvase · 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
- Elsewhere: RCSB PDB 2FCO · PDBe 2FCO
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