3S1C
Maize cytokinin oxidase/dehydrogenase complexed with N6-isopentenyladenosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005576 | cellular_component | extracellular region |
A | 0009690 | biological_process | cytokinin metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019139 | molecular_function | cytokinin dehydrogenase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071949 | molecular_function | FAD binding |
Functional Information from PROSITE/UniProt
site_id | PS00862 |
Number of Residues | 37 |
Details | OX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PaavlypsStaDLvalLsaanstpgwpytIafrGRGH |
Chain | Residue | Details |
A | PRO69-HIS105 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 180 |
Details | Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 13 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15321719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W1O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1W1Q","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15321719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W1R","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Pros-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"15321719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W1O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1W1Q","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15321719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W1O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1W1Q","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18571199","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BW7","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 115 |
Chain | Residue | Details |
A | HIS105 | alter redox potential, covalently attached |
A | ASP169 | electrostatic stabiliser, hydrogen bond acceptor |
A | GLU288 | activator, hydrogen bond donor |