4CZT
Crystal structure of the kinase domain of CIPK23
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 | 0005267 | molecular_function | potassium channel activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007165 | biological_process | signal transduction |
A | 0007584 | biological_process | response to nutrient |
A | 0009414 | biological_process | response to water deprivation |
A | 0009536 | cellular_component | plastid |
A | 0010118 | biological_process | stomatal movement |
A | 0010119 | biological_process | regulation of stomatal movement |
A | 0071805 | biological_process | potassium ion transmembrane transport |
A | 0106310 | molecular_function | protein serine kinase activity |
A | 1990573 | biological_process | potassium ion import across plasma membrane |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005267 | molecular_function | potassium channel activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006468 | biological_process | protein phosphorylation |
B | 0007165 | biological_process | signal transduction |
B | 0007584 | biological_process | response to nutrient |
B | 0009414 | biological_process | response to water deprivation |
B | 0009536 | cellular_component | plastid |
B | 0010118 | biological_process | stomatal movement |
B | 0010119 | biological_process | regulation of stomatal movement |
B | 0071805 | biological_process | potassium ion transmembrane transport |
B | 0106310 | molecular_function | protein serine kinase activity |
B | 1990573 | biological_process | potassium ion import across plasma membrane |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0005267 | molecular_function | potassium channel activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006468 | biological_process | protein phosphorylation |
C | 0007165 | biological_process | signal transduction |
C | 0007584 | biological_process | response to nutrient |
C | 0009414 | biological_process | response to water deprivation |
C | 0009536 | cellular_component | plastid |
C | 0010118 | biological_process | stomatal movement |
C | 0010119 | biological_process | regulation of stomatal movement |
C | 0071805 | biological_process | potassium ion transmembrane transport |
C | 0106310 | molecular_function | protein serine kinase activity |
C | 1990573 | biological_process | potassium ion import across plasma membrane |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005267 | molecular_function | potassium channel activity |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0005886 | cellular_component | plasma membrane |
D | 0006468 | biological_process | protein phosphorylation |
D | 0007165 | biological_process | signal transduction |
D | 0007584 | biological_process | response to nutrient |
D | 0009414 | biological_process | response to water deprivation |
D | 0009536 | cellular_component | plastid |
D | 0010118 | biological_process | stomatal movement |
D | 0010119 | biological_process | regulation of stomatal movement |
D | 0071805 | biological_process | potassium ion transmembrane transport |
D | 0106310 | molecular_function | protein serine kinase activity |
D | 1990573 | biological_process | potassium ion import across plasma membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CPS A 1316 |
Chain | Residue |
A | ALA58 |
A | ASP172 |
A | HIS189 |
A | HOH2051 |
A | HOH2060 |
A | HOH2061 |
C | SER121 |
C | CPS1314 |
A | LEU108 |
A | GLU109 |
A | PHE110 |
A | THR112 |
A | GLY113 |
A | GLY114 |
A | LEU161 |
A | SER171 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CPS B 1314 |
Chain | Residue |
B | VAL45 |
B | GLU109 |
B | PHE110 |
B | GLY113 |
B | SER171 |
B | ASP172 |
B | HOH2063 |
B | HOH2067 |
B | HOH2104 |
B | HOH2107 |
D | SER121 |
D | CPS1325 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CPS C 1314 |
Chain | Residue |
A | GLU115 |
A | ASP118 |
A | SER121 |
A | CPS1316 |
A | HOH2063 |
C | GLU109 |
C | GLY114 |
C | ASP118 |
C | LEU161 |
C | SER171 |
C | ASP172 |
C | LEU175 |
C | LEU187 |
C | HOH2033 |
C | HOH2062 |
C | HOH2065 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CPS D 1325 |
Chain | Residue |
B | CPS1314 |
D | LEU108 |
D | GLU109 |
D | VAL111 |
D | THR112 |
D | GLY113 |
D | GLY114 |
D | GLU115 |
D | LEU161 |
D | SER171 |
D | ASP172 |
D | HIS189 |
D | HOH2075 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CPS D 1326 |
Chain | Residue |
B | ILE203 |
B | THR238 |
B | PHE245 |
C | TYR151 |
C | ALA211 |
C | HOH2074 |
D | ILE203 |
D | ASN204 |
D | LYS206 |
D | THR238 |
D | CPS1327 |
D | HOH2148 |
D | HOH2149 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CPS D 1327 |
Chain | Residue |
C | THR273 |
D | TYR241 |
D | LYS246 |
D | GLU248 |
D | CPS1326 |
D | HOH2114 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CPS C 1315 |
Chain | Residue |
A | ASN236 |
A | THR238 |
C | LYS71 |
C | ILE203 |
C | ASN204 |
C | ASN205 |
C | LEU237 |
C | THR238 |
C | TYR241 |
C | HOH2111 |
C | HOH2112 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 1328 |
Chain | Residue |
D | PHE110 |
D | VAL111 |
D | THR112 |
D | ASP163 |
D | ALA164 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1317 |
Chain | Residue |
A | PRO179 |
A | GLN180 |
A | GLN181 |
A | HOH2145 |
C | ASP234 |
C | SER235 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 1316 |
Chain | Residue |
C | THR112 |
C | ASP163 |
C | ALA164 |
C | HOH2008 |
C | VAL111 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 1317 |
Chain | Residue |
C | SER256 |
C | ALA257 |
C | SER258 |
C | HOH2092 |
C | HOH2113 |
D | LYS260 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 1329 |
Chain | Residue |
B | SER235 |
D | ASP154 |
D | GLN180 |
D | ARG183 |
D | HOH2069 |
D | HOH2079 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 1330 |
Chain | Residue |
D | LYS127 |
D | GLU128 |
D | HOH2053 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1318 |
Chain | Residue |
A | VAL111 |
A | THR112 |
A | ASP163 |
A | ALA164 |
B | LYS288 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1331 |
Chain | Residue |
D | ARG25 |
D | LYS44 |
D | ARG322 |
D | HOH2005 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1319 |
Chain | Residue |
A | LYS64 |
A | ASP311 |
A | HOH2025 |
A | HOH2026 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1332 |
Chain | Residue |
D | PHE249 |
D | CYS251 |
D | LYS260 |
D | LYS264 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 1318 |
Chain | Residue |
C | LYS261 |
C | ARG265 |
C | ASN283 |
C | GLU284 |
C | HOH2106 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1320 |
Chain | Residue |
A | SER235 |
A | ASN236 |
A | HOH2147 |
C | ARG183 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 1319 |
Chain | Residue |
C | LYS64 |
C | ASP311 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1321 |
Chain | Residue |
A | SER256 |
A | ALA257 |
A | SER258 |
A | HOH2128 |
A | HOH2149 |
D | LYS69 |
site_id | CC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 1315 |
Chain | Residue |
B | LYS64 |
B | ASP310 |
site_id | CC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1316 |
Chain | Residue |
B | ASN70 |
B | PRO179 |
B | GLN180 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1317 |
Chain | Residue |
A | LYS87 |
A | ARG93 |
B | SER256 |
B | ALA257 |
B | SER258 |
B | HOH2155 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1333 |
Chain | Residue |
D | LYS64 |
D | ASP310 |
D | ASP311 |
D | HOH2035 |
site_id | CC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 D 1334 |
Chain | Residue |
A | GLY20 |
A | ILE21 |
B | ARG49 |
D | ARG25 |
D | GLY34 |
D | ARG35 |
D | THR36 |
D | LYS46 |
site_id | CC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 1322 |
Chain | Residue |
A | ARG125 |
A | TRP254 |
site_id | DC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 1320 |
Chain | Residue |
C | LYS260 |
C | LYS264 |
C | HOH2087 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGTFAKVKfArnvengdn..........VAIK |
Chain | Residue | Details |
A | LEU37-LYS60 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VyHrDLKpeNLLL |
Chain | Residue | Details |
A | VAL150-LEU162 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP154 | |
B | ASP154 | |
C | ASP154 | |
D | ASP154 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU37 | |
A | LYS60 | |
B | LEU37 | |
B | LYS60 | |
C | LEU37 | |
C | LYS60 | |
D | LEU37 | |
D | LYS60 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q93V58 |
Chain | Residue | Details |
A | SER176 | |
B | SER176 | |
C | SER176 | |
D | SER176 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q38997 |
Chain | Residue | Details |
A | THR190 | |
B | THR190 | |
C | THR190 | |
D | THR190 |