Structure of PDB 1xh4 Chain A

Receptor sequence

>1xh4A (length=337) Species: 9913 (Bos taurus) [Search protein sequence]

SVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHM
ETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDN
SNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLI
YRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSK
GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSS
DLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAP
FIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF

3D structure

PDB

1xh4 Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants

Chain

Resolution

2.45 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	D166 K168 E170 N171 D184 T201
Catalytic site (residue number reindexed from 1)	D153 K155 E157 N158 D171 T188
Enzyme Commision number	2.7.11.11: cAMP-dependent protein kinase.

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	peptide	A	Q84 H87 E127 F129 R133 K168 E170 F187 T197 L198 C199 G200 E203 E230 Y235 F239 D241 D328 Y330	Q71 H74 E114 F116 R120 K155 E157 F174 T184 L185 C186 G187 E190 E217 Y222 F226 D228 D315 Y317
BS02	R69	A	G50 T51 G52 S53 F54 R56 V57 A70 K72 L74 Q84 E91 V123 E127 E170 N171 L173 T183 D184 G186 F327	G37 T38 G39 S40 F41 R43 V44 A57 K59 L61 Q71 E78 V110 E114 E157 N158 L160 T170 D171 G173 F314	MOAD: Kd=34nM PDBbind-CN: -logKd/Ki=7.47,Kd=34nM BindingDB: IC50=30nM

Gene Ontology

	Molecular Function
GO:0004672	protein kinase activity
GO:0004674	protein serine/threonine kinase activity
GO:0004679	AMP-activated protein kinase activity
GO:0004691	cAMP-dependent protein kinase activity
GO:0005515	protein binding
GO:0005524	ATP binding
GO:0019904	protein domain specific binding
GO:0034237	protein kinase A regulatory subunit binding
GO:0106310	protein serine kinase activity

	Biological Process
GO:0001707	mesoderm formation
GO:0006468	protein phosphorylation
GO:0010737	protein kinase A signaling
GO:0016310	phosphorylation
GO:0018105	peptidyl-serine phosphorylation
GO:0034605	cellular response to heat
GO:1904262	negative regulation of TORC1 signaling

	Cellular Component
GO:0001669	acrosomal vesicle
GO:0005634	nucleus
GO:0005737	cytoplasm
GO:0005739	mitochondrion
GO:0005829	cytosol
GO:0005886	plasma membrane
GO:0005952	cAMP-dependent protein kinase complex
GO:0031594	neuromuscular junction
GO:0036126	sperm flagellum
GO:0048471	perinuclear region of cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1xh4, PDBe:1xh4, PDBj:1xh4
PDBsum	1xh4
PubMed	15634010
UniProt	P00517\|KAPCA_BOVIN cAMP-dependent protein kinase catalytic subunit alpha (Gene Name=PRKACA)

[Back to BioLiP]