Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6KE3

Crystal structure of the alpha bata heterodimer of human IDH3 in complex with NADH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005975	biological_process	carbohydrate metabolic process
A	0006099	biological_process	tricarboxylic acid cycle
A	0006102	biological_process	isocitrate metabolic process
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	0045242	cellular_component	isocitrate dehydrogenase complex (NAD+)
A	0046872	molecular_function	metal ion binding
A	0051287	molecular_function	NAD binding
B	0000287	molecular_function	magnesium ion binding
B	0006099	biological_process	tricarboxylic acid cycle
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0051287	molecular_function	NAD binding
C	0000287	molecular_function	magnesium ion binding
C	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005975	biological_process	carbohydrate metabolic process
C	0006099	biological_process	tricarboxylic acid cycle
C	0006102	biological_process	isocitrate metabolic process
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	0045242	cellular_component	isocitrate dehydrogenase complex (NAD+)
C	0046872	molecular_function	metal ion binding
C	0051287	molecular_function	NAD binding
D	0000287	molecular_function	magnesium ion binding
D	0006099	biological_process	tricarboxylic acid cycle
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0051287	molecular_function	NAD binding
E	0000287	molecular_function	magnesium ion binding
E	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0005975	biological_process	carbohydrate metabolic process
E	0006099	biological_process	tricarboxylic acid cycle
E	0006102	biological_process	isocitrate metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0045242	cellular_component	isocitrate dehydrogenase complex (NAD+)
E	0046872	molecular_function	metal ion binding
E	0051287	molecular_function	NAD binding
F	0000287	molecular_function	magnesium ion binding
F	0006099	biological_process	tricarboxylic acid cycle
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0051287	molecular_function	NAD binding
G	0000287	molecular_function	magnesium ion binding
G	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005739	cellular_component	mitochondrion
G	0005759	cellular_component	mitochondrial matrix
G	0005975	biological_process	carbohydrate metabolic process
G	0006099	biological_process	tricarboxylic acid cycle
G	0006102	biological_process	isocitrate metabolic process
G	0016491	molecular_function	oxidoreductase activity
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0045242	cellular_component	isocitrate dehydrogenase complex (NAD+)
G	0046872	molecular_function	metal ion binding
G	0051287	molecular_function	NAD binding
H	0000287	molecular_function	magnesium ion binding
H	0006099	biological_process	tricarboxylic acid cycle
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue NAI A 401

Chain	Residue
A	ILE15
A	GLY264
A	THR265
A	ALA266
A	ASP268
A	ILE269
A	ASN276
B	ASN186
A	LEU72
A	THR74
A	ASN84
A	LEU243
A	GLY244
A	GLU260
A	VAL262
A	HIS263

site_id	AC2
Number of Residues	10
Details	binding site for residue NAI E 401

Chain	Residue
E	LEU72
E	THR74
E	ASN84
E	HIS263
E	GLY264
E	THR265
E	ALA266
E	ALA275
E	ASN276
F	ILE215

site_id	AC3
Number of Residues	13
Details	binding site for residue NAI G 401

Chain	Residue
G	PRO71
G	LEU72
G	THR74
G	ASN84
G	GLU260
G	VAL262
G	HIS263
G	GLY264
G	THR265
G	ALA266
G	ASN276
H	ASN186
H	ASN218

site_id	AC4
Number of Residues	20
Details	binding site for Di-peptide NAI C 401 and ASN C 276

Chain	Residue
C	PRO71
C	LEU72
C	ASN84
C	GLY244
C	GLU260
C	HIS263
C	GLY264
C	THR265
C	ALA266
C	ILE269
C	MET274
C	ALA275
C	PRO277
C	THR278
C	THR315
C	ASP317
C	LEU318
D	ASN186
D	ILE215
D	ASN218

site_id	AC5
Number of Residues	21
Details	binding site for Di-peptide NAI C 401 and ASN C 84

Chain	Residue
C	PRO71
C	LEU72
C	SER82
C	MET83
C	LEU85
C	LEU86
C	LEU87
C	ARG88
C	GLY244
C	GLU260
C	HIS263
C	GLY264
C	THR265
C	ALA266
C	ILE269
C	MET274
C	ALA275
C	ASN276
D	ASN186
D	ILE215
D	ASN218

Functional Information from PROSITE/UniProt

site_id	PS00470
Number of Residues	20
Details	IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDlcAgli.GGLGV

Chain	Residue	Details
A	ASN226-VAL245
B	ASN237-VAL256

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28098230","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Site: {"description":"Critical for catalysis","evidences":[{"source":"PubMed","id":"28098230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28139779","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Critical for catalysis","evidences":[{"source":"PubMed","id":"28098230","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D6R2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9D6R2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D6R2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D6R2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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