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1LLQ

Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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
A0008152biological_processmetabolic process
A0008948molecular_functionoxaloacetate decarboxylase activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0003824molecular_functioncatalytic activity
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
B0008152biological_processmetabolic process
B0008948molecular_functionoxaloacetate decarboxylase activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD A 1001
ChainResidue
AASN275
AILE362
AALA405
ASER406
AVAL408
ALEU432
ASER433
AASN434
AGLY459
AGLY477
AASN479
ATHR299
AHOH2013
APHE326
AGLY327
AALA328
AGLY329
AALA330
AALA331
AASP361

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD B 1002
ChainResidue
BASN275
BTHR299
BPHE326
BALA328
BGLY329
BALA330
BALA331
BASP361
BILE362
BALA405
BSER406
BVAL408
BLEU432
BSER433
BASN434
BGLY459
BGLY477
BASN479

Functional Information from PROSITE/UniProt
site_idPS00331
Number of Residues17
DetailsMALIC_ENZYMES Malic enzymes signature. FnDDiqGTAsViVAGLL
ChainResidueDetails
APHE292-LEU308

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR126
BTYR126

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ALYS199
BLYS199

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:12853453
ChainResidueDetails
AGLN78
AARG81
AARG105
BGLN78
BARG81
BARG105

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12033925, ECO:0000269|PubMed:12853453
ChainResidueDetails
AARG181
AASP295
AGLY327
AASN434
BARG181
BASP295
BGLY327
BASN434

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLU271
AASP272
BGLU271
BASP272

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for activity
ChainResidueDetails
AASP295
BASP295

218853

PDB entries from 2024-04-24

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