Research workbench
Clpap ENGAGED1 state bound to repa-GFP
Analyse Clpap ENGAGED1 state bound to repa-GFP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W1Z
- Type
- protein
- Length
- 6,180 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- S1IIE7, P0ABH9
- Ligands
- ATP, ADP
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G, H, I, J, K, L, M, N, O, P, Q, R, S, T | — | protein | 192 | — | S1IIE7 |
| A, B, C, D, E, F | — | protein | 578 | — | P0ABH9 |
| X | — | protein | 24 | — | — |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 8 copies · chains A, F, B, C, D, E
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6W1Z · ClpAP Engaged1 State bound to RepA-GFP · the same entry in another collection · chain Q against Q, 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 S1IIE7
- Every structure of UniProt P0ABH9
- Elsewhere: RCSB PDB 6W1Z · PDBe 6W1Z · UniProt S1IIE7 · UniProt P0ABH9
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