Research workbench
The structure of the M53A mutant of the caulobacter crescentus clps in complex with a peptide containing an amino-terminal norleucine residue
Analyse The structure of the M53A mutant of the caulobacter crescentus clps in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3G3P
- Type
- protein
- Length
- 166 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease adapter protein clps; Peptide (NLE)LFVQRDSKE
- UniProt
- Q9A5I0
- Ligands
- MG
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP-dependent clp protease adapter protein clps | protein | 82 | 52% helix, 23% strand | Q9A5I0 |
| D | Peptide (NLE)LFVQRDSKE | protein | 2 | 0% helix, 0% strand | — |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.37 | 0.74 | 21 | empty |
| 2 | 53 | 0.25 | 0.73 | 13 | empty |
Interfaces
2 interfaces between chains.
- A–B · 507 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 248 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 3G3P · The structure of the M53A Mutant of the Caulobacter crescentus CLPS in complex with a… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9A5I0 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease adapter protein clps… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9A5I0
- Elsewhere: RCSB PDB 3G3P · PDBe 3G3P · UniProt Q9A5I0
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