Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QR6

HUMAN MITOCHONDRIAL NAD(P)-DEPENDENT MALIC ENZYME

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004470	molecular_function	malic enzyme activity
A	0004471	molecular_function	malate dehydrogenase (decarboxylating) (NAD+) activity
A	0004473	molecular_function	malate dehydrogenase (decarboxylating) (NADP+) activity
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006108	biological_process	malate metabolic process
A	0008948	molecular_function	oxaloacetate decarboxylase activity
A	0009055	molecular_function	electron transfer activity
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	0046872	molecular_function	metal ion binding
A	0051287	molecular_function	NAD binding
A	1902031	biological_process	regulation of NADP metabolic process
B	0003824	molecular_function	catalytic activity
B	0004470	molecular_function	malic enzyme activity
B	0004471	molecular_function	malate dehydrogenase (decarboxylating) (NAD+) activity
B	0004473	molecular_function	malate dehydrogenase (decarboxylating) (NADP+) activity
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006108	biological_process	malate metabolic process
B	0008948	molecular_function	oxaloacetate decarboxylase activity
B	0009055	molecular_function	electron transfer activity
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	0046872	molecular_function	metal ion binding
B	0051287	molecular_function	NAD binding
B	1902031	biological_process	regulation of NADP metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD A 601

Chain	Residue
A	ARG165
A	PHE344
A	ASP345
A	LYS346
A	VAL392
A	ALA393
A	GLY394
A	LEU398
A	LEU419
A	SER420
A	ASN421
A	ASN259
A	GLY446
A	GLY465
A	ASN467
A	HOH2008
A	HOH2048
A	HOH2275
A	HOH2398
A	THR283
A	LEU310
A	GLY311
A	ALA312
A	GLY313
A	GLU314
A	ALA315

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD A 602

Chain	Residue
A	HIS154
A	LYS156
A	GLY192
A	ILE193
A	ARG194
A	ARG197
A	ILE479
A	LEU480
A	ASN482
A	ARG542
A	ARG556
A	HOH2233
A	HOH2301
A	HOH2302
A	HOH2324
A	HOH2510
A	HOH2542
A	HOH2631
B	THR1243
B	ASP1244
B	ARG1248
B	ARG1484

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD B 1601

Chain	Residue
B	ARG1165
B	ASN1259
B	THR1283
B	GLY1311
B	ALA1312
B	GLY1313
B	GLU1314
B	ALA1315
B	ASP1345
B	LYS1346
B	VAL1392
B	ALA1393
B	GLY1394
B	ALA1395
B	LEU1419
B	SER1420
B	ASN1421
B	GLY1446
B	GLY1465
B	ASN1467
B	HOH2035
B	HOH2046
B	HOH2093
B	HOH2173
B	HOH2326
B	HOH2673

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD B 1602

Chain	Residue
A	THR243
A	ASP244
A	GLY247
A	ARG248
A	ARG484
B	HIS1154
B	LYS1156
B	GLY1192
B	ILE1193
B	ARG1194
B	ARG1197
B	ILE1479
B	LEU1480
B	ASN1482
B	ARG1542
B	ARG1556
B	HOH2017
B	HOH2129
B	HOH2352
B	HOH2676
B	HOH2721

Functional Information from PROSITE/UniProt

site_id	PS00331
Number of Residues	17
Details	MALIC_ENZYMES Malic enzymes signature. FnDDiqGTAaVaLAGLL

Chain	Residue	Details
A	PHE276-LEU292

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12962632","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12962632","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12121650","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12962632","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GZ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GZ4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10700286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12962632","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DO8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QR6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10700286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12121650","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12962632","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DO8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GZ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GZ4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10700286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12962632","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DO8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QR6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1DO8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QR6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1DO8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QR6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12962632","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PJ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PJ4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	10
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1do8

Chain	Residue	Details
A	ASP278
A	LYS183
A	TYR112

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1do8

Chain	Residue	Details
B	LYS1183
B	ASP1278
B	TYR1112

site_id	MCSA1
Number of Residues	8
Details	M-CSA 21

Chain	Residue	Details
A	SER136	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ALA189	electrostatic stabiliser, hydrogen bond donor
A	ALA211	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	LEU291	metal ligand
A	LEU292	metal ligand
A	GLU314	hydrogen bond acceptor, proton acceptor, proton donor
A	ALA315	metal ligand
A	GLY473	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	8
Details	M-CSA 21

Chain	Residue	Details
B	SER1136	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ALA1189	electrostatic stabiliser, hydrogen bond donor
B	ALA1211	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	LEU1291	metal ligand
B	LEU1292	metal ligand
B	GLU1314	hydrogen bond acceptor, proton acceptor, proton donor
B	ALA1315	metal ligand
B	GLY1473	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)