Structure of PDB 4ajs Chain A

Receptor sequence
>4ajsA (length=415) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
ESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDA
AVEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIMG
PLTTPVGGGIRSLNVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVI
FRENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPC
SEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLARE
EFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIAC
MNLNGDYISDALAAQVGGIGIAPGANIGDECALFEATHGTAPKYAGQDKV
NPGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAK
LLKCSEFGDAIIENM
3D structure
PDB4ajs Induced Fit and the Catalytic Mechanism of Isocitrate Dehydrogenase.
ChainA
Resolution1.802 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 D283 D307 D311
Catalytic site (residue number reindexed from 1) Y159 K229 D282 D306 D310
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 A2P A H339 G340 A342 Y345 N352 Y391 D392 R395 H338 G339 A341 Y344 N351 Y390 D391 R394
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004450 isocitrate dehydrogenase (NADP+) activity
GO:0005515 protein binding
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
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle
GO:0006979 response to oxidative stress
GO:0022900 electron transport chain
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4ajs, PDBe:4ajs, PDBj:4ajs
PDBsum4ajs
PubMed22891681
UniProtP08200|IDH_ECOLI Isocitrate dehydrogenase [NADP] (Gene Name=icd)

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