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Xchem group deposition -- crystal structure of human ACVR1 in complex with FM007391C

Analyse Xchem group deposition -- crystal structure of human ACVR1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5S7O
Type: protein
Length: 582 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q04771
Ligands: LU8, XJJ, SO4

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	287	—	Q04771
B	—	protein	295	—	Q04771

Ligands and binding sites

LU8 · 4-methyl-3-[4-(1-methylpiperidin-4-yl)phenyl]-5-(3,4,5-trimethoxyphenyl)pyridine · ligand · 4 copies · chains A, B
XJJ · piperazin-2-one · ligand · chains B
SO4 · Sulfate ion · ion · 4 copies · chains A, B
EDO · 1,2-ethanediol · additive · 12 copies · chains A, B
TLA · L(+)-tartaric acid · additive · chains A
DMS · Dimethyl sulfoxide · additive · chains B

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

Compared structures

5S7O · XChem group deposition -- Crystal Structure of human ACVR1 in complex with FM007391c · the same entry in another collection · chain A against A, TM-score 1.00
Q04771 · AlphaFold monomer V2.0 prediction for activin receptor type-1 (Q04771) · a predicted model of the same protein · chain B 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 Q04771
Elsewhere: RCSB PDB 5S7O · PDBe 5S7O · UniProt Q04771

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