6QPL
Crystal structure of Spindlin1 in complex with the inhibitor MS31
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0007276 | biological_process | gamete generation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue MPD B 301 |
| Chain | Residue |
| B | GLY153 |
| B | MET154 |
| B | GLU171 |
| B | VAL242 |
| B | VAL255 |
| B | HOH424 |
| B | HOH432 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MPD B 302 |
| Chain | Residue |
| B | TYR98 |
| B | HOH486 |
| B | TRP62 |
| B | TRP72 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 303 |
| Chain | Residue |
| B | PRO81 |
| B | TYR185 |
| B | LYS186 |
| B | GLY188 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue DMS B 304 |
| Chain | Residue |
| B | JC5305 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue JC5 B 305 |
| Chain | Residue |
| B | ASP95 |
| B | HIS139 |
| B | PHE141 |
| B | TRP151 |
| B | TYR170 |
| B | TYR177 |
| B | TYR179 |
| B | ASP184 |
| B | DMS304 |
| B | HOH425 |
| B | HOH487 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue GLY B 306 |
| Chain | Residue |
| B | ARG191 |
| B | GLN269 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 307 |
| Chain | Residue |
| B | GLU101 |
| B | ARG107 |
| B | GLY146 |
| B | HOH415 |
| B | HOH422 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 308 |
| Chain | Residue |
| B | ASP224 |
| B | GLY225 |
| B | SER226 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 63 |
| Details | Region: {"description":"Tudor-like domain 1","evidences":[{"source":"PubMed","id":"23077255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24589551","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Region: {"description":"Histone H3K4me3 and H3R8me2a binding","evidences":[{"source":"PubMed","id":"23077255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24589551","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 61 |
| Details | Region: {"description":"Tudor-like domain 2","evidences":[{"source":"PubMed","id":"23077255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24589551","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Histone H3K4me3 and H3R8me2a binding","evidences":[{"source":"PubMed","id":"23077255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24589551","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by AURKA","evidences":[{"source":"PubMed","id":"22258766","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
