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Bifunctional DNA PRIMASE/POLYMERASE domain of ORF904 from the archaeal plasmid PRN1- triple mutant F50M/L107M/L110M manganese soak
Analyse Bifunctional DNA PRIMASE/POLYMERASE domain of ORF904 from the archaeal plasmid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RO2
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein ORF904
- UniProt
- Q54324
- Ligands
- ZN, MN
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein ORF904 | protein | 210 | 36% helix, 22% strand | Q54324 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.53 | 0.74 | 36 | MN |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1RO2 · Bifunctional DNA primase/polymerase domain of ORF904 from the archaeal plasmid pRN1… · 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 Q54324
- Elsewhere: RCSB PDB 1RO2 · PDBe 1RO2 · UniProt Q54324
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