MolNFT v1 · #166462 · protein
CLPA/CLPP engaged state bound to repa-GFP
6UQO: “CLPA/CLPP engaged state bound to repa-GFP”. Electron microscopy, 2 ligands (AGS, ADP). MolNFT v1 #166462 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UQO
- Type
- protein
- Length
- 6,174 residues
- Chains
- 22
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A4S4P650, A0A4V3YU15
- Ligands
- AGS, ADP
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 578 | — | A0A4S4P650 |
| G, H, I, J, K, L, M, N, O, P, Q, R, S, T | — | protein | 192 | — | A0A4V3YU15 |
| X, Y | — | protein | 9 | — | — |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 7 copies · chains A, B, C, D, E
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, F, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UQO · ClpA/ClpP Engaged State bound to RepA-GFP · the same entry in another collection · chain C against C, 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 A0A4S4P650
- Every structure of UniProt A0A4V3YU15
- Elsewhere: RCSB PDB 6UQO · PDBe 6UQO · UniProt A0A4S4P650 · UniProt A0A4V3YU15
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