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6UM4

Crystal structure of malate dehydrogenase from Naegleria fowleri ATCC 30863

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006108biological_processmalate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016615molecular_functionmalate dehydrogenase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0003824molecular_functioncatalytic activity
B0006108biological_processmalate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016615molecular_functionmalate dehydrogenase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0003824molecular_functioncatalytic activity
C0006108biological_processmalate metabolic process
C0016491molecular_functionoxidoreductase activity
C0016615molecular_functionmalate dehydrogenase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0003824molecular_functioncatalytic activity
D0006108biological_processmalate metabolic process
D0016491molecular_functionoxidoreductase activity
D0016615molecular_functionmalate dehydrogenase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E0003824molecular_functioncatalytic activity
E0006108biological_processmalate metabolic process
E0016491molecular_functionoxidoreductase activity
E0016615molecular_functionmalate dehydrogenase activity
E0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0003824molecular_functioncatalytic activity
F0006108biological_processmalate metabolic process
F0016491molecular_functionoxidoreductase activity
F0016615molecular_functionmalate dehydrogenase activity
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G0003824molecular_functioncatalytic activity
G0006108biological_processmalate metabolic process
G0016491molecular_functionoxidoreductase activity
G0016615molecular_functionmalate dehydrogenase activity
G0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H0003824molecular_functioncatalytic activity
H0006108biological_processmalate metabolic process
H0016491molecular_functionoxidoreductase activity
H0016615molecular_functionmalate dehydrogenase activity
H0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
I0003824molecular_functioncatalytic activity
I0006108biological_processmalate metabolic process
I0016491molecular_functionoxidoreductase activity
I0016615molecular_functionmalate dehydrogenase activity
I0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
J0003824molecular_functioncatalytic activity
J0006108biological_processmalate metabolic process
J0016491molecular_functionoxidoreductase activity
J0016615molecular_functionmalate dehydrogenase activity
J0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
K0003824molecular_functioncatalytic activity
K0006108biological_processmalate metabolic process
K0016491molecular_functionoxidoreductase activity
K0016615molecular_functionmalate dehydrogenase activity
K0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
L0003824molecular_functioncatalytic activity
L0006108biological_processmalate metabolic process
L0016491molecular_functionoxidoreductase activity
L0016615molecular_functionmalate dehydrogenase activity
L0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue EDO D 501
ChainResidue
DTYR364
DGLU388
KASP304

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO J 501
ChainResidue
ATYR364
JASP304
JGLN306

site_idAC3
Number of Residues2
Detailsbinding site for residue EDO J 502
ChainResidue
AASP304
JTYR364

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO L 501
ChainResidue
CGLN306
LTYR364
LGLU388
LHOH618
CASP304

239803

PDB entries from 2025-08-06

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