Research workbench
Crystal structure of RNase am php domain
Analyse Crystal structure of RNase am php domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UG9
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-3' exoribonuclease
- EC
- 3.1.13.-
- UniProt
- J7Q776
- Ligands
- MN, SO4
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5'-3' exoribonuclease (EC 3.1.13.-) | protein | 206 | 37% helix, 21% strand | J7Q776 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7UG9 · Crystal structure of RNase AM PHP domain · 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 J7Q776
- Elsewhere: RCSB PDB 7UG9 · PDBe 7UG9 · UniProt J7Q776
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