Structure of PDB 1civ Chain A

Receptor sequence
>1civA (length=374) Species: 4224 (Flaveria bidentis) [Search protein sequence]
LPAKQKPECFGVFCLTYDLKAEEETKSWKKIINVAVSGAAGMISNHLLFK
LASGEVFGPDQPISLKLLGSERSFAALEGVAMELEDSLYPLLRQVSIGID
PYEIFQDAEWALLIGAKPRGPGMERADLLDINGQIFAEQGKALNAVASPN
VKVMVVGNPCNTNALICLKNAPNIPPKNFHALTRLDENRAKCQLALKAGV
FYDKVSNVTIWGNHSTTQVPDFLNAKIHGIPVTEVIRDRKWLEDEFTNMV
QTRGGVLIKKWGRSSAASTAVSIVDAIRSLVTPTPEGDWFSTGVYTNGNP
YGIAEDIVFSMPCRSKGDGDYEFVKDVIFDDYLSKKIKKSEDELLAEKKC
VAHLTGEGIAVCDLPEDTMLPGEM
3D structure
PDB1civ Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D197 H225
Catalytic site (residue number reindexed from 1) D186 H214
Enzyme Commision number 1.1.1.82: malate dehydrogenase (NADP(+)).
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 A G49 A51 G52 M53 I54 G80 S81 S84 A127 V167 G168 N169 H225 E384 M385 G38 A40 G41 M42 I43 G69 S70 S73 A116 V156 G157 N158 H214 E373 M374
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016491 oxidoreductase activity
GO:0016615 malate dehydrogenase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046554 L-malate dehydrogenase (NADP+) activity
Biological Process
GO:0006108 malate metabolic process
GO:0019752 carboxylic acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1civ, PDBe:1civ, PDBj:1civ
PDBsum1civ
PubMed10196131
UniProtP46489|MDHP_FLABI Malate dehydrogenase [NADP], chloroplastic

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