Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8KIB

NADP+-dependent cytosolic isocitrate dehydrogenase complexed with oxaloacetate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0005829	cellular_component	cytosol
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0006102	biological_process	isocitrate metabolic process
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0006739	biological_process	NADP metabolic process
A	0006740	biological_process	NADPH regeneration
A	0006749	biological_process	glutathione metabolic process
A	0006979	biological_process	response to oxidative stress
A	0008585	biological_process	female gonad development
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0048545	biological_process	response to steroid hormone
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
A	0060696	biological_process	regulation of phospholipid catabolic process
A	0071071	biological_process	regulation of phospholipid biosynthetic process
B	0000287	molecular_function	magnesium ion binding
B	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005777	cellular_component	peroxisome
B	0005782	cellular_component	peroxisomal matrix
B	0005829	cellular_component	cytosol
B	0006097	biological_process	glyoxylate cycle
B	0006099	biological_process	tricarboxylic acid cycle
B	0006102	biological_process	isocitrate metabolic process
B	0006103	biological_process	2-oxoglutarate metabolic process
B	0006739	biological_process	NADP metabolic process
B	0006740	biological_process	NADPH regeneration
B	0006749	biological_process	glutathione metabolic process
B	0006979	biological_process	response to oxidative stress
B	0008585	biological_process	female gonad development
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0048545	biological_process	response to steroid hormone
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
B	0060696	biological_process	regulation of phospholipid catabolic process
B	0071071	biological_process	regulation of phospholipid biosynthetic process
C	0000287	molecular_function	magnesium ion binding
C	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005777	cellular_component	peroxisome
C	0005782	cellular_component	peroxisomal matrix
C	0005829	cellular_component	cytosol
C	0006097	biological_process	glyoxylate cycle
C	0006099	biological_process	tricarboxylic acid cycle
C	0006102	biological_process	isocitrate metabolic process
C	0006103	biological_process	2-oxoglutarate metabolic process
C	0006739	biological_process	NADP metabolic process
C	0006740	biological_process	NADPH regeneration
C	0006749	biological_process	glutathione metabolic process
C	0006979	biological_process	response to oxidative stress
C	0008585	biological_process	female gonad development
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	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0048545	biological_process	response to steroid hormone
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
C	0060696	biological_process	regulation of phospholipid catabolic process
C	0071071	biological_process	regulation of phospholipid biosynthetic process
D	0000287	molecular_function	magnesium ion binding
D	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005777	cellular_component	peroxisome
D	0005782	cellular_component	peroxisomal matrix
D	0005829	cellular_component	cytosol
D	0006097	biological_process	glyoxylate cycle
D	0006099	biological_process	tricarboxylic acid cycle
D	0006102	biological_process	isocitrate metabolic process
D	0006103	biological_process	2-oxoglutarate metabolic process
D	0006739	biological_process	NADP metabolic process
D	0006740	biological_process	NADPH regeneration
D	0006749	biological_process	glutathione metabolic process
D	0006979	biological_process	response to oxidative stress
D	0008585	biological_process	female gonad development
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	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0048545	biological_process	response to steroid hormone
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding
D	0060696	biological_process	regulation of phospholipid catabolic process
D	0071071	biological_process	regulation of phospholipid biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00470
Number of Residues	20
Details	IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDsvAqgy.GSLGM

Chain	Residue	Details
A	ASN271-MET290

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:29923039, ECO:0007744\|PDB:5YZH, ECO:0007744\|PDB:5YZI

Chain	Residue	Details
A	THR75
B	ASN328
C	THR75
C	ARG82
C	LYS260
C	GLY310
C	ASN328
D	THR75
D	ARG82
D	LYS260
D	GLY310
A	ARG82
D	ASN328
A	LYS260
A	GLY310
A	ASN328
B	THR75
B	ARG82
B	LYS260
B	GLY310

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: in other chain => ECO:0000269\|PubMed:29923039, ECO:0007744\|PDB:5YZI

Chain	Residue	Details
A	THR77
C	SER94
C	ARG109
C	ARG132
D	THR77
D	SER94
D	ARG109
D	ARG132
A	SER94
A	ARG109
A	ARG132
B	THR77
B	SER94
B	ARG109
B	ARG132
C	THR77

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:29923039, ECO:0007744\|PDB:5YZI

Chain	Residue	Details
A	LYS212
B	LYS212
C	LYS212
D	LYS212

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305\|PubMed:29923039

Chain	Residue	Details
A	ASP252
B	ASP252
C	ASP252
D	ASP252

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: in other chain => ECO:0000305\|PubMed:29923039

Chain	Residue	Details
A	ASP275
A	ASP279
B	ASP275
B	ASP279
C	ASP275
C	ASP279
D	ASP275
D	ASP279

site_id	SWS_FT_FI6
Number of Residues	8
Details	SITE: Critical for catalysis => ECO:0000250

Chain	Residue	Details
A	TYR139
A	LYS212
B	TYR139
B	LYS212
C	TYR139
C	LYS212
D	TYR139
D	LYS212

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N-acetylserine => ECO:0000250\|UniProtKB:O75874

Chain	Residue	Details
A	SER2
B	SER2
C	SER2
D	SER2

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:O75874

Chain	Residue	Details
A	TYR42
B	TYR42
C	TYR42
D	TYR42

site_id	SWS_FT_FI9
Number of Residues	16
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:23576753

Chain	Residue	Details
A	LYS81
C	LYS224
C	LYS233
C	LYS243
D	LYS81
D	LYS224
D	LYS233
D	LYS243
A	LYS224
A	LYS233
A	LYS243
B	LYS81
B	LYS224
B	LYS233
B	LYS243
C	LYS81

site_id	SWS_FT_FI10
Number of Residues	8
Details	MOD_RES: N6-succinyllysine => ECO:0007744\|PubMed:23806337

Chain	Residue	Details
A	LYS126
A	LYS400
B	LYS126
B	LYS400
C	LYS126
C	LYS400
D	LYS126
D	LYS400

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:O75874

Chain	Residue	Details
A	LYS321
B	LYS321
C	LYS321
D	LYS321

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:21183079

Chain	Residue	Details
A	SER389
B	SER389
C	SER389
D	SER389

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