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1VL6

Crystal structure of NAD-dependent malic enzyme (TM0542) from Thermotoga maritima at 2.61 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004470molecular_functionmalic enzyme activity
A0004473molecular_functionmalate dehydrogenase (decarboxylating) (NADP+) 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
B0000166molecular_functionnucleotide binding
B0004470molecular_functionmalic enzyme activity
B0004473molecular_functionmalate dehydrogenase (decarboxylating) (NADP+) 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
C0000166molecular_functionnucleotide binding
C0004470molecular_functionmalic enzyme activity
C0004473molecular_functionmalate dehydrogenase (decarboxylating) (NADP+) activity
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0046872molecular_functionmetal ion binding
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0004470molecular_functionmalic enzyme activity
D0004473molecular_functionmalate dehydrogenase (decarboxylating) (NADP+) activity
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0046872molecular_functionmetal ion binding
D0051287molecular_functionNAD binding
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
AASP154
ATYR32
ALYS87

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
BASP154
BTYR32
BLYS87

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
CASP154
CTYR32
CLYS87

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
DASP154
DTYR32
DLYS87

246031

PDB entries from 2025-12-10

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