1D7K
CRYSTAL STRUCTURE OF HUMAN ORNITHINE DECARBOXYLASE AT 2.1 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001822 | biological_process | kidney development |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004586 | molecular_function | ornithine decarboxylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006595 | biological_process | polyamine metabolic process |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0008283 | biological_process | cell population proliferation |
| A | 0008284 | biological_process | positive regulation of cell population proliferation |
| A | 0009615 | biological_process | response to virus |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0033387 | biological_process | putrescine biosynthetic process from ornithine |
| A | 0042176 | biological_process | regulation of protein catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0001822 | biological_process | kidney development |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004586 | molecular_function | ornithine decarboxylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005575 | cellular_component | cellular_component |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006595 | biological_process | polyamine metabolic process |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0008283 | biological_process | cell population proliferation |
| B | 0008284 | biological_process | positive regulation of cell population proliferation |
| B | 0009615 | biological_process | response to virus |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0033387 | biological_process | putrescine biosynthetic process from ornithine |
| B | 0042176 | biological_process | regulation of protein catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PROSITE/UniProt
| site_id | PS00878 |
| Number of Residues | 19 |
| Details | ODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAvKCNdskaIVktLaatG |
| Chain | Residue | Details |
| A | TYR66-GLY84 |
| site_id | PS00879 |
| Number of Residues | 18 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. GaevgfsMyLLDIGGGFP |
| Chain | Residue | Details |
| A | GLY222-PRO239 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor; shared with dimeric partner => ECO:0000305|PubMed:10623504 |
| Chain | Residue | Details |
| A | CYS360 | |
| B | CYS360 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17407445, ECO:0007744|PDB:2OO0 |
| Chain | Residue | Details |
| A | SER200 | |
| A | GLY237 | |
| B | SER200 | |
| B | GLY237 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:26305948, ECO:0000269|PubMed:26443277, ECO:0007744|PDB:2OO0 |
| Chain | Residue | Details |
| A | GLU274 | |
| A | TYR389 | |
| B | GLU274 | |
| B | TYR389 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: in other chain => ECO:0000250|UniProtKB:P07805 |
| Chain | Residue | Details |
| A | TYR331 | |
| B | TYR331 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07805 |
| Chain | Residue | Details |
| A | ASP361 | |
| B | ASP361 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates => ECO:0000250|UniProtKB:P00860 |
| Chain | Residue | Details |
| A | HIS197 | |
| B | HIS197 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:26305948, ECO:0000305|PubMed:17407445 |
| Chain | Residue | Details |
| A | LLP69 | |
| B | LLP69 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P00860 |
| Chain | Residue | Details |
| A | SER303 | |
| B | SER303 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: S-nitrosocysteine; in inhibited form => ECO:0000305|PubMed:11461922 |
| Chain | Residue | Details |
| A | CYS360 | |
| B | CYS360 |
