Research workbench

The complex crystals structure of the FAF1 UBL1_L-HSP70 nbd with ADP and phosphate

Analyse The complex crystals structure of the FAF1 UBL1_L-HSP70 nbd with ADP and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FGM
Type: protein
Length: 460 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P0DMV8, Q9UNN5
Ligands: ADP, MG, PO4

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	379	—	P0DMV8
B	—	protein	81	—	Q9UNN5

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7FGM · The complex crystals structure of the FAF1 UBL1_L-Hsp70 NBD with ADP and phosphate · the same entry in another collection · chain A against A, TM-score 1.00
P0DMV8 · AlphaFold monomer V2.0 prediction for heat shock 70 kda protein 1A (P0DMV8) · a predicted model of the same protein · chain A against A, TM-score 0.90
Q9UNN5 · AlphaFold monomer V2.0 prediction for fas-associated factor 1 (Q9UNN5) · a predicted model of the same protein · chain B against A, TM-score 0.87

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 P0DMV8
Every structure of UniProt Q9UNN5
Elsewhere: RCSB PDB 7FGM · PDBe 7FGM · UniProt P0DMV8 · UniProt Q9UNN5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.