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2DVM

NAD complex structure of PH1275 protein from Pyrococcus horikoshii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004470molecular_functionmalic enzyme 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
B0003824molecular_functioncatalytic activity
B0004470molecular_functionmalic enzyme 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
C0003824molecular_functioncatalytic activity
C0004470molecular_functionmalic enzyme 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
D0003824molecular_functioncatalytic activity
D0004470molecular_functionmalic enzyme activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0046872molecular_functionmetal ion binding
D0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00331
Number of Residues17
DetailsMALIC_ENZYMES Malic enzymes signature. FhDDqqGTAaVvLAGLL
ChainResidueDetails
APHE158-LEU174

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
ATYR38
AASP160
ALYS93

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
BTYR38
BASP160
BLYS93

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
CTYR38
CASP160
CLYS93

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1do8
ChainResidueDetails
DTYR38
DASP160
DLYS93

226262

PDB entries from 2024-10-16

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