5X1C
Crystal Structure of Human CRMP-2 without C-terminal Tail
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227 |
| Chain | Residue | Details |
| A | TYR32 | |
| B | TYR32 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O08553 |
| Chain | Residue | Details |
| A | LYS258 | |
| B | LYS258 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47942 |
| Chain | Residue | Details |
| A | SER259 | |
| B | SER259 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O08553 |
| Chain | Residue | Details |
| A | TYR431 | |
| B | TYR431 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08553 |
| Chain | Residue | Details |
| A | SER465 | |
| B | SER465 |
