Research workbench
Cryo-EM structure of E.COLI ftsh protease cytosolic domains
Analyse Cryo-EM structure of E.COLI ftsh protease cytosolic domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WI4
- Type
- protein
- Length
- 2,460 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AAI3
- Ligands
- ANP, ZN, MG
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E, F, B, C | — | protein | 410 | — | P0AAI3 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 6 copies · chains A, D, E, F, B, C
- ZN · Zinc ion · metal · 6 copies · chains A, D, E, F, B, C
- MG · Magnesium ion · metal · 6 copies · chains A, D, E, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WI4 · Cryo-EM structure of E.Coli FtsH protease cytosolic domains · the same entry in another collection · chain C against C, TM-score 1.00
- P0AAI3 · AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (P0AAI3) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P0AAI3
- Elsewhere: RCSB PDB 7WI4 · PDBe 7WI4 · UniProt P0AAI3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.