1ZTH
Crystal Structure of A.fulgidus Rio1 serine protein kinase bound to ADP and Manganese ion
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030490 | biological_process | maturation of SSU-rRNA |
| A | 0030688 | cellular_component | preribosome, small subunit precursor |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106310 | molecular_function | protein serine kinase activity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030490 | biological_process | maturation of SSU-rRNA |
| B | 0030688 | cellular_component | preribosome, small subunit precursor |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0106310 | molecular_function | protein serine kinase activity |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0030490 | biological_process | maturation of SSU-rRNA |
| C | 0030688 | cellular_component | preribosome, small subunit precursor |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0106310 | molecular_function | protein serine kinase activity |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0030490 | biological_process | maturation of SSU-rRNA |
| D | 0030688 | cellular_component | preribosome, small subunit precursor |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 902 |
| Chain | Residue |
| A | ASN201 |
| A | ASP212 |
| A | ADP901 |
| A | HOH942 |
| A | HOH1073 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 904 |
| Chain | Residue |
| B | HOH1090 |
| B | ASN201 |
| B | ASP212 |
| B | ADP903 |
| B | HOH911 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN C 906 |
| Chain | Residue |
| C | ASN201 |
| C | ASP212 |
| C | ADP905 |
| C | HOH1063 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 908 |
| Chain | Residue |
| D | ASN201 |
| D | ASP212 |
| D | ADP907 |
| D | HOH948 |
| D | HOH1049 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ADP A 901 |
| Chain | Residue |
| A | ILE55 |
| A | SER56 |
| A | VAL63 |
| A | ALA78 |
| A | LYS80 |
| A | PRO135 |
| A | MSE147 |
| A | GLU148 |
| A | PHE149 |
| A | ILE150 |
| A | PRO156 |
| A | ASN201 |
| A | MSE203 |
| A | ILE211 |
| A | ASP212 |
| A | MN902 |
| A | HOH905 |
| A | HOH912 |
| A | HOH915 |
| A | HOH926 |
| A | HOH942 |
| A | HOH955 |
| A | HOH971 |
| A | HOH990 |
| A | HOH1016 |
| A | HOH1073 |
| B | HOH1108 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP B 903 |
| Chain | Residue |
| A | HOH961 |
| B | ILE55 |
| B | SER56 |
| B | VAL63 |
| B | ALA78 |
| B | LYS80 |
| B | PRO135 |
| B | MSE147 |
| B | GLU148 |
| B | PHE149 |
| B | ILE150 |
| B | ASN201 |
| B | ILE211 |
| B | ASP212 |
| B | MN904 |
| B | HOH905 |
| B | HOH910 |
| B | HOH911 |
| B | HOH918 |
| B | HOH922 |
| B | HOH988 |
| B | HOH1008 |
| B | HOH1009 |
| B | HOH1017 |
| B | HOH1073 |
| B | HOH1090 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ADP C 905 |
| Chain | Residue |
| D | HOH979 |
| C | ILE55 |
| C | SER56 |
| C | ALA78 |
| C | LYS80 |
| C | PRO135 |
| C | MSE147 |
| C | GLU148 |
| C | PHE149 |
| C | ILE150 |
| C | PRO156 |
| C | THR159 |
| C | ASN201 |
| C | ILE211 |
| C | ASP212 |
| C | MN906 |
| C | HOH908 |
| C | HOH910 |
| C | HOH912 |
| C | HOH919 |
| C | HOH924 |
| C | HOH928 |
| C | HOH960 |
| C | HOH974 |
| C | HOH1013 |
| C | HOH1028 |
| C | HOH1046 |
| C | HOH1063 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ADP D 907 |
| Chain | Residue |
| C | HOH1085 |
| D | ILE55 |
| D | SER56 |
| D | VAL63 |
| D | ALA78 |
| D | LYS80 |
| D | PRO135 |
| D | MSE147 |
| D | GLU148 |
| D | PHE149 |
| D | ILE150 |
| D | PRO156 |
| D | THR159 |
| D | ASN201 |
| D | ILE211 |
| D | ASP212 |
| D | MN908 |
| D | HOH914 |
| D | HOH915 |
| D | HOH924 |
| D | HOH935 |
| D | HOH943 |
| D | HOH959 |
| D | HOH983 |
| D | HOH986 |
| D | HOH1019 |
| D | HOH1029 |
| D | HOH1049 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9BRS2, ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ASP196 | |
| B | ASP196 | |
| C | ASP196 | |
| D | ASP196 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250|UniProtKB:Q9BRS2 |
| Chain | Residue | Details |
| A | ASP212 | |
| B | ASP212 | |
| C | ASP212 | |
| D | ASP212 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ILE55 | |
| B | ILE55 | |
| C | ILE55 | |
| D | ILE55 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:16008568, ECO:0007744|PDB:1ZP9 |
| Chain | Residue | Details |
| A | LYS80 | |
| B | LYS80 | |
| C | LYS80 | |
| D | LYS80 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16008568, ECO:0007744|PDB:1ZP9 |
| Chain | Residue | Details |
| A | GLU148 | |
| A | ILE150 | |
| B | GLU148 | |
| B | ILE150 | |
| C | GLU148 | |
| C | ILE150 | |
| D | GLU148 | |
| D | ILE150 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O30245 |
| Chain | Residue | Details |
| A | TYR200 | |
| B | TYR200 | |
| C | TYR200 | |
| D | TYR200 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16008568 |
| Chain | Residue | Details |
| A | ASN201 | |
| A | ASP212 | |
| B | ASN201 | |
| B | ASP212 | |
| C | ASN201 | |
| C | ASP212 | |
| D | ASN201 | |
| D | ASP212 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16008568 |
| Chain | Residue | Details |
| A | SER108 | |
| B | SER108 | |
| C | SER108 | |
| D | SER108 |
