Structure of PDB 6bg2 Chain C

Receptor sequence
>6bg2C (length=335) Species: 9606 (Homo sapiens) [Search protein sequence]
EDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKT
FAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYM
LMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLK
PENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHD
ISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKN
AANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPI
IPSVASPTDTSNFDSFPEDNDEPPPDDNSGWDIDF
3D structure
PDB6bg2 Crystal structure of cGMP-dependent protein kinase Ialpha (PKG Ialpha) catalytic domain
ChainC
Resolution1.83 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D484 K486 N489 D502 T521
Catalytic site (residue number reindexed from 1) D148 K150 N153 D166 T185
Enzyme Commision number 2.7.11.12: cGMP-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 ANP C G369 G370 F371 V374 A388 K390 C441 E445 K486 E488 I491 D502 F649 G33 G34 F35 V38 A52 K54 C105 E109 K150 E152 I155 D166 F313
BS02 MN C N489 D502 N153 D166
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004692 cGMP-dependent protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6bg2, PDBe:6bg2, PDBj:6bg2
PDBsum6bg2
PubMed
UniProtQ13976|KGP1_HUMAN cGMP-dependent protein kinase 1 (Gene Name=PRKG1)

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