4ZGY
STRUCTURE of HUMAN ORNITHINE DECARBOXYLASE IN COMPLEX WITH A C-TERMINAL FRAGMENT OF ANTIZYME
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 | 0008073 | molecular_function | ornithine decarboxylase inhibitor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue PLP A 501 |
Chain | Residue |
A | LYS69 |
A | MG502 |
B | PHE192 |
A | ASP88 |
A | ALA111 |
A | HIS197 |
A | GLY237 |
A | GLU274 |
A | GLY276 |
A | ARG277 |
A | TYR389 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | PHE238 |
A | GLY276 |
A | ARG277 |
A | TYR278 |
A | PLP501 |
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 |
site_id | PS01337 |
Number of Residues | 9 |
Details | ODC_AZ Ornithine decarboxylase antizyme signature. LLEFAEEQL |
Chain | Residue | Details |
B | LEU159-LEU167 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor; shared with dimeric partner => ECO:0000305|PubMed:10623504 |
Chain | Residue | Details |
A | CYS360 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17407445, ECO:0007744|PDB:2OO0 |
Chain | Residue | Details |
A | SER200 | |
A | GLY237 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
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 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:P07805 |
Chain | Residue | Details |
A | TYR331 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07805 |
Chain | Residue | Details |
A | ASP361 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates => ECO:0000250|UniProtKB:P00860 |
Chain | Residue | Details |
A | HIS197 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:26305948, ECO:0000305|PubMed:17407445 |
Chain | Residue | Details |
A | LYS69 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P00860 |
Chain | Residue | Details |
A | SER303 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: S-nitrosocysteine; in inhibited form => ECO:0000305|PubMed:11461922 |
Chain | Residue | Details |
A | CYS360 |