7ODC
CRYSTAL STRUCTURE ORNITHINE DECARBOXYLASE FROM MOUSE, TRUNCATED 37 RESIDUES FROM THE C-TERMINUS, TO 1.6 ANGSTROM 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 | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006595 | biological_process | polyamine metabolic process |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0006597 | biological_process | spermine biosynthetic process |
| A | 0008284 | biological_process | positive regulation of cell population proliferation |
| A | 0008295 | biological_process | spermidine biosynthetic process |
| A | 0009446 | biological_process | putrescine biosynthetic process |
| 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 |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 425 |
| Chain | Residue |
| A | GLY237 |
| A | GLU274 |
| A | GLY276 |
| A | ARG277 |
| A | CYS360 |
| A | TYR389 |
| A | HOH686 |
| A | HOH724 |
| A | HOH744 |
| A | ALA67 |
| A | LYS69 |
| A | ASP88 |
| A | ARG154 |
| A | HIS197 |
| A | GLY236 |
| site_id | COF |
| Number of Residues | 1 |
| Details | K69 IS BOUND TO PLP VIA A SCHIFF BASE |
| Chain | Residue |
| A | LYS69 |
| site_id | DIN |
| Number of Residues | 1 |
| Details | DOMAIN INTERFACE |
| Chain | Residue |
| A | GLY387 |
| site_id | SSP |
| Number of Residues | 1 |
| Details | SUBSTRATE SPECIFICITY POCKET |
| Chain | Residue |
| A | ASP361 |
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. YAvKCNdsraIVstLaaiG |
| 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. AtevgfsMhLLDIGGGFP |
| Chain | Residue | Details |
| A | ALA222-PRO239 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor; shared with dimeric partner","evidences":[{"source":"PubMed","id":"10378276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1730582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8504104","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11926","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10378276","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| 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 | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates","evidences":[{"source":"PubMed","id":"10378276","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10378276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1730582","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ODC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P11926","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10378276 |
| Chain | Residue | Details |
| A | GLU274 | |
| A | LYS69 | |
| A | HIS197 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 937 |
| Chain | Residue | Details |
| A | LYS69 | |
| A | HIS197 | |
| A | GLU274 |
