Structure of PDB 6bg2 Chain D

Receptor sequence
>6bg2D (length=328) Species: 9606 (Homo sapiens) [Search protein sequence]
KYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILK
KRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLG
GELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILD
HRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWS
LGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKK
LCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASP
TDTSNFDSFPEDNDEPPPDDNSGWDIDF
3D structure
PDB6bg2 Crystal structure of cGMP-dependent protein kinase Ialpha (PKG Ialpha) catalytic domain
ChainD
Resolution1.83 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) D484 K486 N489 D502 T521
Catalytic site (residue number reindexed from 1) D141 K143 N146 D159 T178
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 D G367 G369 G370 F371 V374 A388 K390 C441 E445 K486 E488 I491 D502 F649 G24 G26 G27 F28 V31 A45 K47 C98 E102 K143 E145 I148 D159 F306
BS02 MN D N489 D502 N146 D159
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

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

[Back to BioLiP]