Structure of PDB 5n23 Chain A

Receptor sequence

>5n23A (length=337) Species: 9606 (Homo sapiens) [Search protein sequence]

KGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIRTLGTGSFGRV
MLVKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRIQQAVNFPFLVKLE
FSFKDNSNLYMVLEYAPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYL
HSLDLIYRDLKPENLLIDQQGYIKVADFGFAKRVKGRTWTLCGTPEYLAP
EIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF
PSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQ
RKVEAPFIPKFSNFDDYEEEEIRVSINEKCGKEFSEF

3D structure

PDB

5n23 Inhibitor induced structural effects involving Phe327 in AGC kinases

Chain

Resolution

2.088 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 N171 D184 T201
Catalytic site (residue number reindexed from 1)	D159 K161 N164 D177 T194
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	S53 E127 F129 R133 E170 L198 G200 T201 P202 E203 E230 Y235 F239 A240 D241 I246	S46 E120 F122 R126 E163 L191 G193 T194 P195 E196 E223 Y228 F232 A233 D234 I239
BS02	35R	A	L49 G50 A70 E121 Y122 A123 G126 S130 L173 F327	L42 G43 A63 E114 Y115 A116 G119 S123 L166 F314

Gene Ontology

	Molecular Function
GO:0004672	protein kinase activity
GO:0004674	protein serine/threonine kinase activity
GO:0005524	ATP binding

	Biological Process
GO:0006468	protein phosphorylation

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:5n23, PDBe:5n23, PDBj:5n23
PDBsum	5n23
PubMed
UniProt	P17612\|KAPCA_HUMAN cAMP-dependent protein kinase catalytic subunit alpha (Gene Name=PRKACA)

[Back to BioLiP]