5YZA
Crystal Structure of Human CRMP-2 with S522D mutation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004157 | molecular_function | dihydropyrimidinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005874 | cellular_component | microtubule |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006208 | biological_process | pyrimidine nucleobase catabolic process |
| A | 0006897 | biological_process | endocytosis |
| A | 0007010 | biological_process | cytoskeleton organization |
| A | 0007165 | biological_process | signal transduction |
| A | 0007399 | biological_process | nervous system development |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| A | 0030154 | biological_process | cell differentiation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227 |
| Chain | Residue | Details |
| A | TYR32 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O08553 |
| Chain | Residue | Details |
| A | LYS258 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47942 |
| Chain | Residue | Details |
| A | SER259 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O08553 |
| Chain | Residue | Details |
| A | TYR431 | |
| A | TYR499 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08553 |
| Chain | Residue | Details |
| A | SER465 | |
| A | SER507 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P47942 |
| Chain | Residue | Details |
| A | CYS504 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:10757975, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR509 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O08553 |
| Chain | Residue | Details |
| A | THR512 | |
| A | THR521 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by GSK3-beta => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | THR514 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER517 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:10757975, ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER518 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by DYRK2 => ECO:0000269|PubMed:10757975, ECO:0000269|PubMed:15466863, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | ASP522 |
