Structure of PDB 2iv0 Chain A

Receptor sequence
>2iv0A (length=412) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence]
MQYEKVKPPENGEKIRYENGKLIVPDNPIIPYFEGDGIGKDVVPAAIRVL
DAAADKIGKEVVWFQVYAGEDAYKLYGNYLPDDTLNAIKEFRVALKGPLT
TPVGGGYRSLNVTIRQVLDLYANVRPVYYLKGVPSPIKHPEKVNFVIFRE
NTEDVYAGIEWPRGSEEALKLIRFLKNEFGVTIREDSGIGIKPISEFATK
RLVRMAIRYAIENNRKSVTLVHKGNIMKYTEGAFRDWGYEVAKQEFGEYC
ITEDELWDKYGGKQPEGKIVVKDRIADNMFQQILTRTDEYDVIALPNLNG
DYLSDAAAALIGGLGIAPGSNIGDGIGVFEPVHGSAPKYAGQNKVNPTAE
ILTGALMFEYIGWKDASEMIKKAVEMTISSGIVTYDIHRHMGGTKVGTRE
FAEAVVENLQSL
3D structure
PDB2iv0 Thermal Stability of Isocitrate Dehydrogenase from Archaeoglobus Fulgidus Studied by Crystal Structure Analysis and Engineering of Chimers
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y156 K223 D277 D301 D305
Catalytic site (residue number reindexed from 1) Y156 K223 D277 D301 D305
Enzyme Commision number 1.1.1.42: isocitrate 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 ZN A H388 G393 H388 G393
BS02 ZN A D301 D305 D301 D305
Gene Ontology
Molecular Function
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
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Biological Process
External links
PDB RCSB:2iv0, PDBe:2iv0, PDBj:2iv0
PDBsum2iv0
PubMed17401542
UniProtO29610|IDH_ARCFU Isocitrate dehydrogenase [NADP] (Gene Name=icd)

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