1FYR
DIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTAL STRUCTURE OF THE GRB2-SH2 AC-PYVNV COMPLEX
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACE I -1 |
| Chain | Residue |
| A | ARG67 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACE J -1 |
| Chain | Residue |
| B | ARG67 |
| J | HOH1039 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACE K -1 |
| Chain | Residue |
| C | ARG67 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACE L -1 |
| Chain | Residue |
| D | ARG67 |
| L | HOH1031 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258 |
| Chain | Residue | Details |
| I | PTR0 | |
| J | PTR0 | |
| K | PTR0 | |
| L | PTR0 | |
| C | LYS50 | |
| C | LYS109 | |
| D | LYS50 | |
| D | LYS109 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:34348893 |
| Chain | Residue | Details |
| A | LYS109 | |
| B | LYS109 | |
| C | LYS109 | |
| D | LYS109 |
