Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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	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	0009507	cellular_component	chloroplast
A	0009536	cellular_component	plastid
A	0010118	biological_process	stomatal movement
A	0010119	biological_process	regulation of stomatal movement
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	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	0009507	cellular_component	chloroplast
B	0009536	cellular_component	plastid
B	0010118	biological_process	stomatal movement
B	0010119	biological_process	regulation of stomatal movement
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	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	0009507	cellular_component	chloroplast
C	0009536	cellular_component	plastid
C	0010118	biological_process	stomatal movement
C	0010119	biological_process	regulation of stomatal movement
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	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	0009507	cellular_component	chloroplast
D	0009536	cellular_component	plastid
D	0010118	biological_process	stomatal movement
D	0010119	biological_process	regulation of stomatal movement
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	1020
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	116
Details	Region: {"description":"Activation loop","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q93V58","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q38997","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)