Research workbench
KEAP1 - peptide complex
Analyse KEAP1 - peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FMQ
- Type
- protein
- Length
- 575 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q14145
- Ligands
- ACE, DYW, NA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 285 | — | Q14145 |
| D | — | protein | 5 | — | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains D
- DYW · (2~{S})-1-[(2~{S})-2-azanyl-4-oxidanyl-4-oxidanylidene-butanoyl]pyrrolidine-2-carboxylic acid · ligand · chains A, B, D
- NA · Sodium ion · metal · 7 copies · chains A, B, D
- ACT · Acetate ion · additive · 7 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FMQ · Keap1 - peptide complex · the same entry in another collection · chain A against A, 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 Q14145
- Elsewhere: RCSB PDB 6FMQ · PDBe 6FMQ · UniProt Q14145
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