Research workbench
S. aureus mazf in complex with substrate analogue
Analyse S. aureus mazf in complex with substrate analogue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DLO
- Type
- protein + DNA
- Length
- 121 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoribonuclease mazf; DNA substrate analogue auacaua
- EC
- 3.1.-.-
- UniProt
- A7X4P5
- Ligands
- CL
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoribonuclease mazf (EC 3.1.-.-) | protein | 114 | 20% helix, 38% strand | A7X4P5 |
| B | DNA substrate analogue auacaua | dna | 7 | — | — |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 891 Ų buried · 31 hydrogen bonds · protein-nucleic
Compared structures
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 A7X4P5
- Elsewhere: RCSB PDB 5DLO · PDBe 5DLO · UniProt A7X4P5
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