6Q2Q
Crystal structure of mouse viperin bound to uridine triphosphate and S-adenosylhomocysteine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005811 | cellular_component | lipid droplet |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051607 | biological_process | defense response to virus |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005811 | cellular_component | lipid droplet |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 A 401 |
| Chain | Residue |
| A | CYS84 |
| A | TYR86 |
| A | CYS88 |
| A | CYS91 |
| A | GLY126 |
| A | ASN158 |
| A | ARG194 |
| A | SAH402 |
| A | HOH584 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue SAH A 402 |
| Chain | Residue |
| A | PHE90 |
| A | PHE92 |
| A | SER124 |
| A | GLY125 |
| A | GLY126 |
| A | GLU127 |
| A | VAL156 |
| A | SER157 |
| A | ASN158 |
| A | SER180 |
| A | ARG194 |
| A | ASN222 |
| A | VAL224 |
| A | CYS251 |
| A | LEU252 |
| A | ASN258 |
| A | SF4401 |
| A | UTP404 |
| A | HOH527 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | GLN196 |
| A | GLY197 |
| A | LYS198 |
| A | LYS199 |
| A | HIS201 |
| A | HOH790 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue UTP A 404 |
| Chain | Residue |
| A | ASN77 |
| A | HIS79 |
| A | PHE92 |
| A | LYS120 |
| A | ASN122 |
| A | SER124 |
| A | LYS220 |
| A | ASN222 |
| A | ARG245 |
| A | LYS247 |
| A | PHE249 |
| A | LEU252 |
| A | ILE254 |
| A | LYS299 |
| A | TYR302 |
| A | ILE304 |
| A | LYS319 |
| A | ARG347 |
| A | TYR351 |
| A | SAH402 |
| A | HOH528 |
| A | HOH559 |
| A | HOH567 |
| A | HOH640 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 405 |
| Chain | Residue |
| A | LYS114 |
| B | GLU164 |
| B | TRP211 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue B3P A 406 |
| Chain | Residue |
| A | PRO151 |
| A | SER354 |
| A | ALA356 |
| A | ASP357 |
| A | HOH509 |
| A | HOH523 |
| A | HOH570 |
| A | HOH664 |
| A | HOH734 |
| A | HOH748 |
| A | HOH776 |
| B | ARG213 |
| B | ASP214 |
| B | TYR215 |
| B | LYS216 |
| B | HOH533 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 407 |
| Chain | Residue |
| A | PRO292 |
| A | SER294 |
| A | LYS297 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 B 401 |
| Chain | Residue |
| B | CYS84 |
| B | TYR86 |
| B | CYS88 |
| B | CYS91 |
| B | GLY126 |
| B | ASN158 |
| B | ARG194 |
| B | SAH402 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | binding site for residue SAH B 402 |
| Chain | Residue |
| B | ASN222 |
| B | VAL224 |
| B | PHE249 |
| B | CYS251 |
| B | LEU252 |
| B | ASN258 |
| B | SF4401 |
| B | UTP403 |
| B | HOH556 |
| B | PHE90 |
| B | PHE92 |
| B | SER124 |
| B | GLY125 |
| B | GLY126 |
| B | GLU127 |
| B | VAL156 |
| B | SER157 |
| B | ASN158 |
| B | SER180 |
| B | ARG194 |
| site_id | AD1 |
| Number of Residues | 24 |
| Details | binding site for residue UTP B 403 |
| Chain | Residue |
| B | ASN77 |
| B | HIS79 |
| B | PHE92 |
| B | LYS120 |
| B | ASN122 |
| B | SER124 |
| B | VAL156 |
| B | LYS220 |
| B | ASN222 |
| B | ARG245 |
| B | LYS247 |
| B | PHE249 |
| B | LEU252 |
| B | ILE254 |
| B | TYR302 |
| B | ILE304 |
| B | LYS319 |
| B | ARG347 |
| B | TYR351 |
| B | SAH402 |
| B | HOH517 |
| B | HOH567 |
| B | HOH643 |
| B | HOH677 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 404 |
| Chain | Residue |
| B | SER294 |
| B | LYS297 |
| B | HOH769 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28607080","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5VSL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5VSM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8WXG1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q8WXG1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
