Structure of PDB 3rho Chain D

Receptor sequence
>3rhoD (length=498) Species: 10116 (Rattus norvegicus) [Search protein sequence]
VINYVEKAVNKLTLQMPYQLFIGGEFVDAEGSKTYNTINPTDGSVICQVS
LAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADVMEQHQEELA
TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQARPNR
NLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPL
TALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEV
GKHIMKSCALSNVKKVSLQLGGKSPLIIFADCDLNKAVQMGMSSVFFNKG
ENCIAAGRLFVEESIHNQFVQKVVEEVEKMKIGNPLERDTNHGPQNHEAH
LRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEE
SFGPIMIISRFADGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQ
AGTVFINTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTFEY
3D structure
PDB3rho Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain control binding and discharging of the coenzyme.
ChainD
Resolution2.26 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N574 K597 Q673 C707 E804 D883
Catalytic site (residue number reindexed from 1) N170 K193 Q269 C303 E400 D479
Enzyme Commision number 1.5.1.6: formyltetrahydrofolate dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAP D V570 I571 P572 W573 K597 A599 Q600 S629 G630 G634 Q635 F648 G650 S651 V654 I658 Q673 L674 C707 E804 F806 V166 I167 P168 W169 K193 A195 Q196 S225 G226 G230 Q231 F244 G246 S247 V250 I254 Q269 L270 C303 E400 F402 MOAD: Kd=0.26uM
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

View graph for
Molecular Function
External links
PDB RCSB:3rho, PDBe:3rho, PDBj:3rho
PDBsum3rho
PubMed21540484
UniProtP28037|AL1L1_RAT Cytosolic 10-formyltetrahydrofolate dehydrogenase (Gene Name=Aldh1l1)

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