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 | 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 arginine, via 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 | 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 arginine, via 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 | Active site: {"description":"Proton donor; shared with dimeric partner","evidences":[{"source":"PubMed","id":"10623504","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17407445","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OO0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17407445","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26305948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26443277","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OO0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P07805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates","evidences":[{"source":"UniProtKB","id":"P00860","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"26305948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17407445","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-nitrosocysteine; in inhibited form","evidences":[{"source":"PubMed","id":"11461922","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | LYS161 | |
| A | LLP69 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| B | LYS161 | |
| B | LLP69 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | GLU274 | |
| A | HIS197 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| B | GLU274 | |
| B | HIS197 |
