Structure of PDB 2y7j Chain D

Receptor sequence
>2y7jD (length=281) Species: 9606 (Homo sapiens) [Search protein sequence]
ELPDWAAAKEFYQKYDPKDVIGRGVSSVVRRCVHRATGHEFAVKIMEVRL
SPEQLEEVREATRRETHILRQVAGHPHIITLIDSYESSSFMFLVFDLMRK
GELFDYLTEKVALSEKETRSIMRSLLEAVSFLHANNIVHRDLKPENILLD
DNMQIRLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDETHPGYGK
EVDLWACGVILFTLLAGSPPFWHRRQILMLRMIMEGQYQFSSPEWDDRSS
TVKDLISRLLQVDPEARLTAEQALQHPFFER
3D structure
PDB2y7j Structure of Human Phosphorylase Kinase, Gamma 2
ChainD
Resolution2.5 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) D153 K155 E157 N158 D171 T190
Catalytic site (residue number reindexed from 1) D141 K143 E145 N146 D159 T178
Enzyme Commision number 2.7.11.19: phosphorylase 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 B49 D I30 A51 F107 D108 L109 M110 R111 G113 L160 I21 A42 F95 D96 L97 M98 R99 G101 L148 BindingDB: Kd=5.9nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004689 phosphorylase kinase activity
GO:0005516 calmodulin binding
GO:0005524 ATP binding
GO:0019865 immunoglobulin binding
Biological Process
GO:0005977 glycogen metabolic process
GO:0006468 protein phosphorylation
Cellular Component
GO:0005964 phosphorylase kinase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2y7j, PDBe:2y7j, PDBj:2y7j
PDBsum2y7j
PubMed
UniProtP15735|PHKG2_HUMAN Phosphorylase b kinase gamma catalytic chain, liver/testis isoform (Gene Name=PHKG2)

[Back to BioLiP]