Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1EFK

STRUCTURE OF HUMAN MALIC ENZYME IN COMPLEX WITH KETOMALONATE

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 604

Chain	Residue
A	ARG165
A	GLU255
A	ASP256
A	ASP279
A	MAK603
A	HOH4072

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1604

Chain	Residue
B	ASP279
B	MAK1603
B	HOH4073
B	ARG165
B	GLU255
B	ASP256

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG C 2604

Chain	Residue
C	ARG165
C	LYS183
C	GLU255
C	ASP256
C	ASP279
C	MAK2603
C	HOH4074

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 3604

Chain	Residue
D	ARG165
D	GLU255
D	ASP256
D	ASP279
D	MAK3603
D	HOH4075

site_id	AC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD A 601

Chain	Residue
A	ARG165
A	LEU167
A	GLY168
A	ASN259
A	ASP279
A	THR283
A	LEU310
A	GLY311
A	ALA312
A	GLY313
A	GLU314
A	ALA315
A	ASP345
A	LYS346
A	VAL392
A	ALA393
A	GLY394
A	ALA395
A	LEU419
A	SER420
A	ASN421
A	GLY446
A	GLY465
A	ASN466
A	ASN467
A	MAK603
A	HOH4006

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE NAD A 602

Chain	Residue
A	HIS154
A	ARG194
A	ARG197
A	ILE479
A	LEU480
A	ASN482
A	ARG542
A	TYR552
A	ARG556
D	ASP244
D	ARG245
D	GLY247

site_id	AC7
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD B 1601

Chain	Residue
B	ARG165
B	LEU167
B	GLY168
B	ASN259
B	ASP279
B	THR283
B	GLY311
B	ALA312
B	GLY313
B	GLU314
B	ALA315
B	ASP345
B	LYS346
B	VAL392
B	ALA393
B	GLY394
B	ALA395
B	LEU398
B	LEU419
B	ASN421
B	GLY446
B	GLY465
B	ASN466
B	ASN467
B	MAK1603

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NAD B 1602

Chain	Residue
C	ARG245
B	HIS154
B	LYS156
B	GLY192
B	ILE193
B	ARG194
B	ARG197
B	ILE479
B	ARG542
B	TYR552
B	ARG556

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD C 2601

Chain	Residue
C	ARG165
C	LEU167
C	GLY168
C	ASN259
C	ASP279
C	THR283
C	GLY311
C	ALA312
C	GLY313
C	GLU314
C	ALA315
C	ASP345
C	LYS346
C	VAL392
C	ALA393
C	GLY394
C	ALA395
C	LEU419
C	ASN421
C	GLY446
C	GLY465
C	ASN466
C	ASN467
C	MAK2603

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE NAD C 2602

Chain	Residue
B	ASP244
B	ARG245
C	HIS154
C	LYS156
C	GLY192
C	ILE193
C	ARG194
C	ARG197
C	ILE479
C	LEU480
C	TYR552
C	ARG556

site_id	BC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD D 3601

Chain	Residue
D	ARG165
D	LEU167
D	GLY168
D	ASN259
D	ASP279
D	THR283
D	LEU310
D	GLY311
D	ALA312
D	GLY313
D	GLU314
D	ALA315
D	ASP345
D	LYS346
D	VAL392
D	ALA393
D	GLY394
D	ALA395
D	LEU398
D	LEU419
D	ASN421
D	GLY465
D	ASN466
D	ASN467
D	MAK3603

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NAD D 3602

Chain	Residue
A	ASP244
A	ARG245
D	HIS154
D	ARG194
D	ARG197
D	ILE479
D	LEU480
D	ASN482
D	ARG542
D	TYR552
D	ARG556

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE MAK A 603

Chain	Residue
A	TYR112
A	ARG165
A	LEU167
A	LYS183
A	GLU255
A	ASP256
A	ASP279
A	ASN421
A	ASN466
A	ASN467
A	NAD601
A	MG604
A	HOH4072

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MAK B 1603

Chain	Residue
B	ARG165
B	LEU167
B	LYS183
B	GLU255
B	ASP256
B	ASP279
B	ASN421
B	ASN466
B	ASN467
B	NAD1601
B	MG1604
B	HOH4073

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE MAK C 2603

Chain	Residue
C	TYR112
C	ARG165
C	LEU167
C	LYS183
C	GLU255
C	ASP256
C	ASP279
C	ASN421
C	ASN466
C	ASN467
C	NAD2601
C	MG2604
C	HOH4074

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MAK D 3603

Chain	Residue
D	ARG165
D	LEU167
D	GLU255
D	ASP256
D	ASP279
D	ASN421
D	ASN466
D	ASN467
D	NAD3601
D	MG3604
D	HOH4075

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	4
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:12962632

Chain	Residue	Details
A	TYR112
B	TYR112
C	TYR112
D	TYR112

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:12962632

Chain	Residue	Details
A	LYS183
B	LYS183
C	LYS183
D	LYS183

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:12121650, ECO:0000269\|PubMed:12962632, ECO:0007744\|PDB:1GZ3, ECO:0007744\|PDB:1GZ4, ECO:0007744\|PDB:1PJ2, ECO:0007744\|PDB:1PJ3, ECO:0007744\|PDB:1PJ4

Chain	Residue	Details
A	ARG67
A	ARG91
B	ARG67
B	ARG91
C	ARG67
C	ARG91
D	ARG67
D	ARG91

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10700286, ECO:0000269\|PubMed:12962632, ECO:0007744\|PDB:1DO8, ECO:0007744\|PDB:1EFK, ECO:0007744\|PDB:1EFL, ECO:0007744\|PDB:1PJ3, ECO:0007744\|PDB:1PJL, ECO:0007744\|PDB:1QR6

Chain	Residue	Details
A	ARG165
A	ALA312
B	ARG165
B	ALA312
C	ARG165
C	ALA312
D	ARG165
D	ALA312

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:10700286, ECO:0000269\|PubMed:12121650, ECO:0000269\|PubMed:12962632, ECO:0007744\|PDB:1DO8, ECO:0007744\|PDB:1EFK, ECO:0007744\|PDB:1EFL, ECO:0007744\|PDB:1GZ3, ECO:0007744\|PDB:1GZ4, ECO:0007744\|PDB:1PJ2, ECO:0007744\|PDB:1PJ3, ECO:0007744\|PDB:1PJ4

Chain	Residue	Details
A	GLU255
D	GLU255
D	ASP256
D	ASP279
A	ASP256
A	ASP279
B	GLU255
B	ASP256
B	ASP279
C	GLU255
C	ASP256
C	ASP279

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:10700286, ECO:0000269\|PubMed:12962632, ECO:0007744\|PDB:1DO8, ECO:0007744\|PDB:1EFK, ECO:0007744\|PDB:1EFL, ECO:0007744\|PDB:1PJ3, ECO:0007744\|PDB:1QR6

Chain	Residue	Details
A	ASN259
B	ASN259
C	ASN259
D	ASN259

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744\|PDB:1DO8, ECO:0007744\|PDB:1EFK, ECO:0007744\|PDB:1EFL, ECO:0007744\|PDB:1PJ3, ECO:0007744\|PDB:1QR6

Chain	Residue	Details
A	GLU314
B	GLU314
C	GLU314
D	GLU314

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744\|PDB:1DO8, ECO:0007744\|PDB:1EFK, ECO:0007744\|PDB:1EFL, ECO:0007744\|PDB:1PJ3, ECO:0007744\|PDB:1PJL, ECO:0007744\|PDB:1QR6

Chain	Residue	Details
A	ALA315
B	ALA315
C	ALA315
D	ALA315

site_id	SWS_FT_FI9
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:12962632, ECO:0007744\|PDB:1PJ2, ECO:0007744\|PDB:1PJ4

Chain	Residue	Details
A	ASN421
A	ASN466
B	ASN421
B	ASN466
C	ASN421
C	ASN466
D	ASN421
D	ASN466

site_id	SWS_FT_FI10
Number of Residues	20
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS156
B	LYS346
C	LYS156
C	LYS224
C	LYS240
C	LYS272
C	LYS346
D	LYS156
D	LYS224
D	LYS240
D	LYS272
A	LYS224
D	LYS346
A	LYS240
A	LYS272
A	LYS346
B	LYS156
B	LYS224
B	LYS240
B	LYS272

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	ASP278
B	LYS183
B	TYR112

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1do8

Chain	Residue	Details
C	ASP278
C	LYS183
C	TYR112

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1do8

Chain	Residue	Details
D	ASP278
D	LYS183
D	TYR112

site_id	MCSA1
Number of Residues	8
Details	M-CSA 21

Chain	Residue	Details
A	ARG140	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ILE193	electrostatic stabiliser, hydrogen bond donor
A	ASP215	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	GLN295	metal ligand
A	LYS296	metal ligand
A	GLY318	hydrogen bond acceptor, proton acceptor, proton donor
A	ILE319	metal ligand
A	ALA477	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	8
Details	M-CSA 21

Chain	Residue	Details
B	ARG140	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ILE193	electrostatic stabiliser, hydrogen bond donor
B	ASP215	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	GLN295	metal ligand
B	LYS296	metal ligand
B	GLY318	hydrogen bond acceptor, proton acceptor, proton donor
B	ILE319	metal ligand
B	ALA477	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	8
Details	M-CSA 21

Chain	Residue	Details
C	ARG140	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ILE193	electrostatic stabiliser, hydrogen bond donor
C	ASP215	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	GLN295	metal ligand
C	LYS296	metal ligand
C	GLY318	hydrogen bond acceptor, proton acceptor, proton donor
C	ILE319	metal ligand
C	ALA477	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	8
Details	M-CSA 21

Chain	Residue	Details
D	ARG140	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ILE193	electrostatic stabiliser, hydrogen bond donor
D	ASP215	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	GLN295	metal ligand
D	LYS296	metal ligand
D	GLY318	hydrogen bond acceptor, proton acceptor, proton donor
D	ILE319	metal ligand
D	ALA477	electrostatic stabiliser, hydrogen bond donor

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