Structure of PDB 2rka Chain A
Receptor sequence
>2rkaA (length=611) Species:
10116
(Rattus norvegicus) [
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QLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEY
GRLLAHMQEEGVIRKLKKYDNCWLALTDPRDVARIESKTVIITQEQRDTV
PIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPL
AKIGIELTDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLK
KPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRIASR
LAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGW
KVECVGDDIAWMKFDAQGNLRAINPENGFFGVAPGTSVKTNPNAIKTIQK
NTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCAHPN
SRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHG
VFVGAAMRSEAKVIMHDPFAMRPFFGYNFGKYLAHWLSMAHRPAAKLPKI
FHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPKE
DALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERE
LRALKQRISQM
3D structure
PDB
2rka
Differential Inhibition of Cytosolic PEPCK by Substrate Analogues. Kinetic and Structural Characterization of Inhibitor Recognition.
Chain
A
Resolution
1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
R87 Y235 K244 H264 S286 C288 D311 R405
Catalytic site (residue number reindexed from 1)
R84 Y232 K241 H261 S283 C285 D308 R402
Enzyme Commision number
2.7.11.-
4.1.1.32
: phosphoenolpyruvate carboxykinase (GTP).
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
PGA
A
R87 G237 K244 F333 R405
R84 G234 K241 F330 R402
MOAD
: Ki=1mM
PDBbind-CN
: -logKd/Ki=3.00,Ki=1mM
BS02
MN
A
K244 H264 D311
K241 H261 D308
BS03
MN
A
H502 E607
H491 E596
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0004550
nucleoside diphosphate kinase activity
GO:0004611
phosphoenolpyruvate carboxykinase activity
GO:0004613
phosphoenolpyruvate carboxykinase (GTP) activity
GO:0005525
GTP binding
GO:0016301
kinase activity
GO:0016831
carboxy-lyase activity
GO:0017076
purine nucleotide binding
GO:0019003
GDP binding
GO:0030145
manganese ion binding
GO:0031406
carboxylic acid binding
GO:0046872
metal ion binding
GO:0106264
protein serine kinase activity (using GTP as donor)
Biological Process
GO:0006006
glucose metabolic process
GO:0006094
gluconeogenesis
GO:0006107
oxaloacetate metabolic process
GO:0006629
lipid metabolic process
GO:0009617
response to bacterium
GO:0014823
response to activity
GO:0016310
phosphorylation
GO:0018105
peptidyl-serine phosphorylation
GO:0019543
propionate catabolic process
GO:0031667
response to nutrient levels
GO:0032496
response to lipopolysaccharide
GO:0032868
response to insulin
GO:0032869
cellular response to insulin stimulus
GO:0033993
response to lipid
GO:0042593
glucose homeostasis
GO:0042594
response to starvation
GO:0043382
positive regulation of memory T cell differentiation
GO:0043648
dicarboxylic acid metabolic process
GO:0045944
positive regulation of transcription by RNA polymerase II
GO:0046166
glyceraldehyde-3-phosphate biosynthetic process
GO:0046327
glycerol biosynthetic process from pyruvate
GO:0046889
positive regulation of lipid biosynthetic process
GO:0046890
regulation of lipid biosynthetic process
GO:0051365
cellular response to potassium ion starvation
GO:0070365
hepatocyte differentiation
GO:0070741
response to interleukin-6
GO:0071300
cellular response to retinoic acid
GO:0071320
cellular response to cAMP
GO:0071332
cellular response to fructose stimulus
GO:0071333
cellular response to glucose stimulus
GO:0071347
cellular response to interleukin-1
GO:0071356
cellular response to tumor necrosis factor
GO:0071377
cellular response to glucagon stimulus
GO:0071456
cellular response to hypoxia
GO:0071474
cellular hyperosmotic response
GO:0071475
cellular hyperosmotic salinity response
GO:0071476
cellular hypotonic response
GO:0071477
cellular hypotonic salinity response
GO:0071549
cellular response to dexamethasone stimulus
GO:0072350
tricarboxylic acid metabolic process
GO:0097403
cellular response to raffinose
GO:1904628
cellular response to phorbol 13-acetate 12-myristate
GO:1904640
response to methionine
Cellular Component
GO:0005737
cytoplasm
GO:0005783
endoplasmic reticulum
GO:0005829
cytosol
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:2rka
,
PDBe:2rka
,
PDBj:2rka
PDBsum
2rka
PubMed
18197707
UniProt
P07379
|PCKGC_RAT Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (Gene Name=Pck1)
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