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 |
C | GLU148 | |
C | ILE150 | |
D | GLU148 | |
D | ILE150 | |
A | GLU148 | |
A | ILE150 | |
B | GLU148 | |
B | ILE150 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O30245 |
Chain | Residue | Details |
D | TYR200 | |
A | TYR200 | |
B | TYR200 | |
C | TYR200 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16008568 |
Chain | Residue | Details |
C | ASN201 | |
C | ASP212 | |
D | ASN201 | |
D | ASP212 | |
A | ASN201 | |
A | ASP212 | |
B | ASN201 | |
B | ASP212 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16008568 |
Chain | Residue | Details |
D | SER108 | |
A | SER108 | |
B | SER108 | |
C | SER108 |