Structure of PDB 2d4v Chain A

Receptor sequence
>2d4vA (length=427) Species: 930 (Acidithiobacillus thiooxidans) [Search protein sequence]
THIQKPATGSPLTLLNGVLQVPDQPIIPFIEGDGIGCDVTPAMRSVVDAA
VAKVYGGQRQIAWMELFAGQKAVQLYGEGQYLPDETMAAIREYKVAIKGP
LETPVGGGIRSLNVAMRQDLDLYVCLRPVRYFEGTPSPMRHPEKVDMVIF
RENSEDIYAGIEWPAGSPEAEKIIRFLREEMGVTKIRFPDSSAIGIKPVS
TEGSERLIRRTIQYALEHGKPSVSLVHKGNIMKFTEGGFRDWGYALAERE
FAGRVFTWRQKAAISKAEGKAAGQKAEQQAIADGKLIIKDVIADNFLQQI
LLRPEDYSVVATLNLNGDYVSDALAAEVGGIGMAPGANLSDTHAIFEATH
GTAPDIAGQGKANPSSLILSAVMMLEHLGWGEAAQAIVAAMNATIAAGEV
TGDLAALRGDVPALSTTEFTAALIRRF
3D structure
PDB2d4v Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y160 K230 D296 D320 D324
Catalytic site (residue number reindexed from 1) Y158 K228 D294 D318 D322
Enzyme Commision number 1.1.1.42: isocitrate dehydrogenase (NADP(+)).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004450 isocitrate dehydrogenase (NADP+) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0051287 NAD binding
Biological Process
GO:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2d4v, PDBe:2d4v, PDBj:2d4v
PDBsum2d4v
PubMed17634983
UniProtQ8GAX0

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