Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4P69

Acek (D477A) ICDH complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006006	biological_process	glucose metabolic process
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0008772	molecular_function	[isocitrate dehydrogenase (NADP+)] kinase activity
A	0016208	molecular_function	AMP binding
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0016791	molecular_function	phosphatase activity
B	0000166	molecular_function	nucleotide binding
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004721	molecular_function	phosphoprotein phosphatase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006006	biological_process	glucose metabolic process
B	0006097	biological_process	glyoxylate cycle
B	0006099	biological_process	tricarboxylic acid cycle
B	0008772	molecular_function	[isocitrate dehydrogenase (NADP+)] kinase activity
B	0016208	molecular_function	AMP binding
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0016791	molecular_function	phosphatase activity
C	0000287	molecular_function	magnesium ion binding
C	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006097	biological_process	glyoxylate cycle
C	0006099	biological_process	tricarboxylic acid cycle
C	0006979	biological_process	response to oxidative stress
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0022900	biological_process	electron transport chain
C	0046872	molecular_function	metal ion binding
C	0051287	molecular_function	NAD binding
C	0097216	molecular_function	guanosine tetraphosphate binding
D	0000287	molecular_function	magnesium ion binding
D	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006097	biological_process	glyoxylate cycle
D	0006099	biological_process	tricarboxylic acid cycle
D	0006979	biological_process	response to oxidative stress
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0022900	biological_process	electron transport chain
D	0046872	molecular_function	metal ion binding
D	0051287	molecular_function	NAD binding
D	0097216	molecular_function	guanosine tetraphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue AMP A 601

Chain	Residue
A	SER101
A	GLU376
A	ASN104
A	SER105
A	HIS113
A	LEU116
A	LYS291
A	LYS294
A	THR295
A	TYR298

site_id	AC2
Number of Residues	17
Details	binding site for residue ADP A 602

Chain	Residue
A	PRO316
A	GLY317
A	ILE318
A	GLY320
A	VAL322
A	MET323
A	VAL325
A	LYS336
A	GLU416
A	ARG417
A	ARG418
A	MET419
A	LYS461
A	ASN462
A	TYR474
A	ASP475
A	ALA477

site_id	AC3
Number of Residues	15
Details	binding site for residue ADP B 601

Chain	Residue
B	ILE318
B	GLY320
B	MET321
B	VAL322
B	MET323
B	VAL325
B	VAL334
B	LYS336
B	GLU416
B	ARG417
B	MET419
B	ASP457
B	LYS461
B	ASN462
B	ASP475

site_id	AC4
Number of Residues	8
Details	binding site for residue AMP B 602

Chain	Residue
B	ASN104
B	SER105
B	HIS113
B	LYS291
B	LYS294
B	THR295
B	TYR298
B	GLU376

site_id	AC5
Number of Residues	9
Details	binding site for Ligand GLU C 87 bound to SER C 3

Chain	Residue
C	SER3
C	VAL5
C	TYR78
C	PRO85
C	ALA86
C	THR88
C	LEU89
C	ASP90
C	LEU91

site_id	AC6
Number of Residues	9
Details	binding site for Ligand GLU C 87 bound to SER C 3

Chain	Residue
C	SER3
C	VAL5
C	TYR78
C	PRO85
C	ALA86
C	THR88
C	LEU89
C	ASP90
C	LEU91

site_id	AC7
Number of Residues	6
Details	binding site for Ligand THR C 271 bound to ASN C 268

Chain	Residue
C	ASP221
C	ASN268
C	PRO269
C	ASN270
C	GLY272
C	LYS273

site_id	AC8
Number of Residues	6
Details	binding site for Ligand ASP C 392 bound to ASN C 352

Chain	Residue
C	ASN352
C	THR390
C	TYR391
C	PHE393
C	GLU394
C	LEU396

site_id	AC9
Number of Residues	11
Details	binding site for Di-peptide TYR C 57 and ARG C 61

Chain	Residue
C	GLU25
C	VAL53
C	GLU54
C	LYS55
C	ALA56
C	LYS58
C	GLY59
C	GLU60
C	LYS62
C	TRP369
C	ALA372

site_id	AD1
Number of Residues	16
Details	binding site for Di-peptide PHE C 178 and PHE D 178

Chain	Residue
D	LYS174
D	VAL175
D	ILE176
D	LYS177
D	LEU179
D	ARG180
D	GLU182
D	MET183
C	LYS174
C	VAL175
C	ILE176
C	LYS177
C	LEU179
C	ARG180
C	GLU182
C	MET183

site_id	AD2
Number of Residues	16
Details	binding site for Di-peptide PHE C 178 and PHE D 178

Chain	Residue
C	LYS174
C	VAL175
C	ILE176
C	LYS177
C	LEU179
C	ARG180
C	GLU182
C	MET183
D	LYS174
D	VAL175
D	ILE176
D	LYS177
D	LEU179
D	ARG180
D	GLU182
D	MET183

site_id	AD3
Number of Residues	16
Details	binding site for Di-peptide PHE C 178 and PHE D 178

Chain	Residue
C	LYS174
C	VAL175
C	ILE176
C	LYS177
C	LEU179
C	ARG180
C	GLU182
C	MET183
D	LYS174
D	VAL175
D	ILE176
D	LYS177
D	LEU179
D	ARG180
D	GLU182
D	MET183

site_id	AD4
Number of Residues	16
Details	binding site for Di-peptide PHE C 178 and PHE D 178

Chain	Residue
C	LYS174
C	VAL175
C	ILE176
C	LYS177
C	LEU179
C	ARG180
C	GLU182
C	MET183
D	LYS174
D	VAL175
D	ILE176
D	LYS177
D	LEU179
D	ARG180
D	GLU182
D	MET183

site_id	AD5
Number of Residues	16
Details	binding site for Di-peptide PHE C 178 and PHE D 178

Chain	Residue
C	LYS174
C	VAL175
C	ILE176
C	LYS177
C	LEU179
C	ARG180
C	GLU182
C	MET183
D	LYS174
D	VAL175
D	ILE176
D	LYS177
D	LEU179
D	ARG180
D	GLU182
D	MET183

site_id	AD6
Number of Residues	16
Details	binding site for Di-peptide PHE C 178 and PHE D 178

Chain	Residue
C	LYS174
C	VAL175
C	ILE176
C	LYS177
C	LEU179
C	ARG180
C	GLU182
C	MET183
D	LYS174
D	VAL175
D	ILE176
D	LYS177
D	LEU179
D	ARG180
D	GLU182
D	MET183

site_id	AD7
Number of Residues	16
Details	binding site for Di-peptide PHE C 178 and PHE D 178

Chain	Residue
C	LYS174
C	VAL175
C	ILE176
C	LYS177
C	LEU179
C	ARG180
C	GLU182
C	MET183
D	LYS174
D	VAL175
D	ILE176
D	LYS177
D	LEU179
D	ARG180
D	GLU182
D	MET183

site_id	AD8
Number of Residues	16
Details	binding site for Di-peptide PHE C 178 and PHE D 178

Chain	Residue
C	LYS174
C	VAL175
C	ILE176
C	LYS177
C	LEU179
C	ARG180
C	GLU182
C	MET183
D	LYS174
D	VAL175
D	ILE176
D	LYS177
D	LEU179
D	ARG180
D	GLU182
D	MET183

site_id	AD9
Number of Residues	9
Details	binding site for Di-peptide ASP C 221 and LYS C 273

Chain	Residue
C	ALA217
C	ILE218
C	ALA219
C	ASN220
C	ARG222
C	ASN268
C	THR271
C	GLY272
C	GLU274

site_id	AE1
Number of Residues	9
Details	binding site for Di-peptide ASP C 221 and LYS C 273

Chain	Residue
C	ALA217
C	ILE218
C	ALA219
C	ASN220
C	ARG222
C	ASN268
C	THR271
C	GLY272
C	GLU274

site_id	AE2
Number of Residues	13
Details	binding site for Di-peptide GLU C 238 and MET C 302

Chain	Residue
C	ASP158
C	LYS199
C	CYS201
C	THR237
C	GLY239
C	ALA240
C	PHE241
C	LYS242
C	CYS301
C	ASN303
C	LEU304
C	ASN305
C	GLY306

site_id	AE3
Number of Residues	29
Details	binding site for Di-peptide ASP C 283 and ASP D 307

Chain	Residue
C	ARG153
C	LYS230
C	ILE281
C	ALA282
C	ALA284
C	PHE285
C	LEU286
C	ASN303
C	LEU304
C	ASN305
C	GLY306
C	TYR308
C	ILE309
C	SER310
C	ASP311
D	ARG153
D	ILE281
D	ALA282
D	ALA284
D	PHE285
D	LEU286
D	ASN303
D	LEU304
D	ASN305
D	GLY306
D	TYR308
D	ILE309
D	SER310
D	ASP311

site_id	AE4
Number of Residues	9
Details	binding site for Di-peptide LYS D 13 and GLU D 94

Chain	Residue
D	LYS12
D	ILE14
D	THR15
D	ASP90
D	LEU91
D	ILE92
D	ARG93
D	TYR95
D	ARG96

site_id	AE5
Number of Residues	12
Details	binding site for Di-peptide TYR D 57 and ARG D 61

Chain	Residue
D	GLU25
D	VAL53
D	LYS55
D	ALA56
D	LYS58
D	GLY59
D	GLU60
D	LYS62
D	TRP369
D	THR370
D	GLU371
D	ALA372

site_id	AE6
Number of Residues	12
Details	binding site for Di-peptide TYR D 78 and GLU D 87

Chain	Residue
D	SER3
D	LYS4
D	SER74
D	VAL77
D	GLY79
D	VAL82
D	PRO85
D	ALA86
D	THR88
D	LEU89
D	ASP90
D	LEU91

site_id	AE7
Number of Residues	12
Details	binding site for Di-peptide TYR D 125 and ARG D 208

Chain	Residue
D	ASP123
D	LEU124
D	ILE126
D	GLU154
D	ASN155
D	GLU204
D	GLY205
D	THR206
D	LYS207
D	LEU209
D	ILE328
D	ASP330

site_id	AE8
Number of Residues	12
Details	binding site for Di-peptide TYR D 125 and ARG D 208

Chain	Residue
D	ASP123
D	LEU124
D	ILE126
D	GLU154
D	ASN155
D	GLU204
D	GLY205
D	THR206
D	LYS207
D	LEU209
D	ILE328
D	ASP330

site_id	AE9
Number of Residues	12
Details	binding site for Di-peptide TYR D 125 and ARG D 208

Chain	Residue
D	ASP123
D	LEU124
D	ILE126
D	GLU154
D	ASN155
D	GLU204
D	GLY205
D	THR206
D	LYS207
D	LEU209
D	ILE328
D	ASP330

site_id	AF1
Number of Residues	12
Details	binding site for Di-peptide TYR D 125 and ARG D 208

Chain	Residue
D	ASP123
D	LEU124
D	ILE126
D	GLU154
D	ASN155
D	GLU204
D	GLY205
D	THR206
D	LYS207
D	LEU209
D	ILE328
D	ASP330

site_id	AF2
Number of Residues	12
Details	binding site for Di-peptide TYR D 125 and ARG D 208

Chain	Residue
D	ASP123
D	LEU124
D	ILE126
D	GLU154
D	ASN155
D	GLU204
D	GLY205
D	THR206
D	LYS207
D	LEU209
D	ILE328
D	ASP330

site_id	AF3
Number of Residues	12
Details	binding site for Di-peptide TYR D 125 and ARG D 208

Chain	Residue
D	ASP123
D	LEU124
D	ILE126
D	GLU154
D	ASN155
D	GLU204
D	GLY205
D	THR206
D	LYS207
D	LEU209
D	ILE328
D	ASP330

site_id	AF4
Number of Residues	12
Details	binding site for Di-peptide TYR D 125 and ARG D 208

Chain	Residue
D	ASP123
D	LEU124
D	ILE126
D	GLU154
D	ASN155
D	GLU204
D	GLY205
D	THR206
D	LYS207
D	LEU209
D	ILE328
D	ASP330

site_id	AF5
Number of Residues	12
Details	binding site for Di-peptide TYR D 125 and ARG D 208

Chain	Residue
D	ASP123
D	LEU124
D	ILE126
D	GLU154
D	ASN155
D	GLU204
D	GLY205
D	THR206
D	LYS207
D	LEU209
D	ILE328
D	ASP330

site_id	AF6
Number of Residues	9
Details	binding site for Di-peptide GLN D 287 and LEU D 291

Chain	Residue
C	ASP311
D	ALA284
D	PHE285
D	LEU286
D	GLN288
D	ILE289
D	LEU290
D	ARG292
D	PRO293

site_id	AF7
Number of Residues	12
Details	binding site for Di-peptide GLU D 361 and ARG D 365

Chain	Residue
D	ASN220
D	ILE357
D	LEU358
D	SER359
D	ALA360
D	MET362
D	MET363
D	LEU364
D	HIS366
D	MET367
D	GLY368
D	ASP374

Functional Information from PROSITE/UniProt

site_id	PS00470
Number of Residues	20
Details	IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI

Chain	Residue	Details
C	ASN303-ILE322

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00747","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00747","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11284679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2682654","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HJ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IDE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10623532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2204109","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AI3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CW1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CW7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GRP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P8F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PB1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BNP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ICD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8ICD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10623532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2204109","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AI3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CW7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GRP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P8F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PB1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BNP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ICD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8ICD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10623532","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CW1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CW4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11284679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2682654","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BL5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HJ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IDE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ISO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9ICD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11284679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2682654","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BL5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HJ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IDE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AJR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9ICD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11284679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2682654","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9ICD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Site: {"description":"Critical for catalysis","evidences":[{"source":"PubMed","id":"7761851","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7819221","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"2204109","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3112144","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 7

Chain	Residue	Details
C	TYR160	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	LYS230	electrostatic stabiliser, proton acceptor, proton donor, proton relay
C	ASP283	electrostatic stabiliser, proton acceptor, proton donor
C	ASP307	metal ligand

site_id	MCSA2
Number of Residues	4
Details	M-CSA 7

Chain	Residue	Details
D	TYR160	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	LYS230	electrostatic stabiliser, proton acceptor, proton donor, proton relay
D	ASP283	electrostatic stabiliser, proton acceptor, proton donor
D	ASP307	metal ligand

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