MolNFT v1 · #173685 · protein
Deampylation complex of monomeric ficd and ampylated bip (state 2)
7B80: “Deampylation complex of monomeric ficd and ampylated bip (state 2)”. X-ray diffraction, 4 ligands (AMP, K, MG). MolNFT v1 #173685 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7B80
- Type
- protein
- Length
- 863 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G3I8R9, Q9BVA6
- Ligands
- AMP, K, MG, PO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 523 | — | G3I8R9 |
| A | — | protein | 340 | — | Q9BVA6 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains B, A
- K · Potassium ion · metal · 3 copies · chains B
- MG · Magnesium ion · metal · 2 copies · chains B, A
- PO4 · Phosphate ion · ion · chains B
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7B80 · DeAMPylation complex of monomeric FICD and AMPylated BiP (state 2) · the same entry in another collection · chain B against B, TM-score 1.00
- G3I8R9 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (G3I8R9) · a predicted model of the same protein · chain B against A, TM-score 0.98
- Q9BVA6 · AlphaFold monomer V2.0 prediction for protein adenylyltransferase ficd (Q9BVA6) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 G3I8R9
- Every structure of UniProt Q9BVA6
- Elsewhere: RCSB PDB 7B80 · PDBe 7B80 · UniProt G3I8R9 · UniProt Q9BVA6
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