Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1QR6

HUMAN MITOCHONDRIAL NAD(P)-DEPENDENT MALIC ENZYME

Functional Information from GO Data
ChainGOidnamespacecontents
A0004470molecular_functionmalic enzyme activity
A0004471molecular_functionmalate dehydrogenase (decarboxylating) (NAD+) activity
A0004473molecular_functionmalate dehydrogenase (decarboxylating) (NADP+) activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006090biological_processpyruvate metabolic process
A0006108biological_processmalate metabolic process
A0008948molecular_functionoxaloacetate decarboxylase activity
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
A1902031biological_processregulation of NADP metabolic process
B0004470molecular_functionmalic enzyme activity
B0004471molecular_functionmalate dehydrogenase (decarboxylating) (NAD+) activity
B0004473molecular_functionmalate dehydrogenase (decarboxylating) (NADP+) activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006090biological_processpyruvate metabolic process
B0006108biological_processmalate metabolic process
B0008948molecular_functionoxaloacetate decarboxylase activity
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
B1902031biological_processregulation of NADP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD A 601
ChainResidue
AARG165
APHE344
AASP345
ALYS346
AVAL392
AALA393
AGLY394
ALEU398
ALEU419
ASER420
AASN421
AASN259
AGLY446
AGLY465
AASN467
AHOH2008
AHOH2048
AHOH2275
AHOH2398
ATHR283
ALEU310
AGLY311
AALA312
AGLY313
AGLU314
AALA315

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD A 602
ChainResidue
AHIS154
ALYS156
AGLY192
AILE193
AARG194
AARG197
AILE479
ALEU480
AASN482
AARG542
AARG556
AHOH2233
AHOH2301
AHOH2302
AHOH2324
AHOH2510
AHOH2542
AHOH2631
BTHR1243
BASP1244
BARG1248
BARG1484

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 1601
ChainResidue
BARG1165
BASN1259
BTHR1283
BGLY1311
BALA1312
BGLY1313
BGLU1314
BALA1315
BASP1345
BLYS1346
BVAL1392
BALA1393
BGLY1394
BALA1395
BLEU1419
BSER1420
BASN1421
BGLY1446
BGLY1465
BASN1467
BHOH2035
BHOH2046
BHOH2093
BHOH2173
BHOH2326
BHOH2673

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD B 1602
ChainResidue
ATHR243
AASP244
AGLY247
AARG248
AARG484
BHIS1154
BLYS1156
BGLY1192
BILE1193
BARG1194
BARG1197
BILE1479
BLEU1480
BASN1482
BARG1542
BARG1556
BHOH2017
BHOH2129
BHOH2352
BHOH2676
BHOH2721

Functional Information from PROSITE/UniProt
site_idPS00331
Number of Residues17
DetailsMALIC_ENZYMES Malic enzymes signature. FnDDiqGTAaVaLAGLL
ChainResidueDetails
APHE276-LEU292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:12962632
ChainResidueDetails
ATYR112
BTYR1112

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:12962632
ChainResidueDetails
ALYS183
BLYS1183

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12121650, ECO:0000269|PubMed:12962632
ChainResidueDetails
AARG67
AARG91
BARG1067
BARG1091

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12962632
ChainResidueDetails
AARG165
AASN421
AASN466
BARG1165
BASN1421
BASN1466

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10700286, ECO:0000269|PubMed:12121650, ECO:0000269|PubMed:12962632
ChainResidueDetails
AGLU255
AASP256
AASP279
BGLU1255
BASP1256
BASP1279

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10700286, ECO:0000269|PubMed:12962632
ChainResidueDetails
AASN259
AGLY311
BASN1259
BGLY1311

site_idSWS_FT_FI7
Number of Residues10
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS156
BLYS1346
ALYS224
ALYS240
ALYS272
ALYS346
BLYS1156
BLYS1224
BLYS1240
BLYS1272

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
AASP278
ALYS183
ATYR112

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
BLYS1183
BASP1278
BTYR1112

site_idMCSA1
Number of Residues8
DetailsM-CSA 21
ChainResidueDetails
ATYR112electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG165electrostatic stabiliser, hydrogen bond donor
ALYS183electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
AGLU255metal ligand
AASP256metal ligand
AASP278hydrogen bond acceptor, proton acceptor, proton donor
AASP279metal ligand
AASN421electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues8
DetailsM-CSA 21
ChainResidueDetails
BTYR1112electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BARG1165electrostatic stabiliser, hydrogen bond donor
BLYS1183electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
BGLU1255metal ligand
BASP1256metal ligand
BASP1278hydrogen bond acceptor, proton acceptor, proton donor
BASP1279metal ligand
BASN1421electrostatic stabiliser, hydrogen bond donor

226262

PDB entries from 2024-10-16

PDB statisticsPDBj update infoContact PDBjnumon