MolNFT v1 · #15003 · protein

Saccharomyces cerevisiae ADP-ribosylation factor 2 (SCARF2) complexed with GDP-3'P at 1.6A resolution

1MR3: “Saccharomyces cerevisiae ADP-ribosylation factor 2 (SCARF2) complexed with GDP-3'P at 1.6A resolution”. X-ray diffraction, 2 ligands (G3D, MG). MolNFT v1 #15003 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1MR3
Type: protein
Length: 177 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosylation factor 2
UniProt: P19146
Ligands: G3D, MG

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F	ADP-ribosylation factor 2	protein	177	34% helix, 29% strand	P19146

Ligands and binding sites

G3D · Guanosine-3'-monophosphate-5'-diphosphate · ligand · chains F
MG · Magnesium ion · metal · chains F
EDO · 1,2-ethanediol · additive · 10 copies · chains F
EOH · Ethanol · additive · 4 copies · chains F
GOL · Glycerol · additive · 2 copies · chains F
PDO · 1,3-propandiol · additive · 2 copies · chains F

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

Compared structures

1MR3 · Saccharomyces cerevisiae ADP-ribosylation Factor 2 (ScArf2) complexed with GDP-3'P at… · the same entry in another collection · chain F against F, TM-score 1.00
P19146 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor 2 (P19146) · a predicted model of the same protein · chain F against A, TM-score 0.80

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 P19146
Elsewhere: RCSB PDB 1MR3 · PDBe 1MR3 · UniProt P19146

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