Structure of PDB 1grp Chain A

Receptor sequence
>1grpA (length=414) Species: 562 (Escherichia coli) [Search protein sequence]
SKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAA
VEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGP
LTTPVGGGIRSLLVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIF
RENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPDHCGIGIKPCS
EEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLAREE
FGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACM
NLNGDYISDALAAQVGGIGIAPGANIGDECALFEATHGTAPKYAGQDKVN
PGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKL
LKCSEFGDAIIENM
3D structure
PDB1grp Second-site suppression of regulatory phosphorylation in Escherichia coli isocitrate dehydrogenase.
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) Y160 K230 D283 D307 D311
Catalytic site (residue number reindexed from 1) Y158 K228 D281 D305 D309
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 MG A D307 D311 D305 D309
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1grp, PDBe:1grp, PDBj:1grp
PDBsum1grp
PubMed8745407
UniProtP08200|IDH_ECOLI Isocitrate dehydrogenase [NADP] (Gene Name=icd)

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