Research workbench
Mycoplasma genitalium dnak deletion mutant lacking sbdalpha in complex with ADP and pi.
Analyse Mycoplasma genitalium dnak deletion mutant lacking sbdalpha in complex with ADP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OBV
- Type
- protein
- Length
- 520 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P47547
- Ligands
- ADP, PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 520 | — | P47547 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OBV · Mycoplasma genitalium DnaK deletion mutant lacking SBDalpha in complex with ADP and Pi. · the same entry in another collection · chain A against A, TM-score 1.00
- P47547 · AlphaFold monomer V2.0 prediction for chaperone protein dnak (P47547) · a predicted model of the same protein · chain A against A, TM-score 0.65
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 P47547
- Elsewhere: RCSB PDB 5OBV · PDBe 5OBV · UniProt P47547
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