Structure of PDB 3qr0 Chain A

Receptor sequence
>3qr0A (length=781) Species: 6610 (Sepia officinalis) [Search protein sequence]
IELKWPKVPEQLIKGDKFLKWEEGSSGFIEILLRVDPKGYFLYWKIEGKE
DTQLLDLAYVRDIRCAKYAKPPKDKKIKEAGTNFGSSNIPLQDKCVTICH
GYNYIDLEWTHLVAENSSVAKKWSEEVFSYAYNLLSLNKNQLGEWEKLYF
RLTTVEMEKNKIPVKAIQKCLSKDKDDRARISKALEKIGWPSGKNDAIDL
KAFDFDTFFKFYLALLERSEIEGIFKELSKNKGNITTVMFRDFLNDMQRH
PSLHKTLFPLYTDAQCEALINDYESAVNKKGKKKGQLTKEGLLYFLMCEE
NNLTPMHRLDLGANMKLTLAAYYINSSHNTYLTGHQLTGKSSVEIYRQVL
LTGCRCLELDCWDGKDGEPIITHGFTMCTEVLFKDVVYAIAESAFKVSDY
PVILSFENHCSVAQQKLLAQYCNEAFGELLLDKPIDGHPLKPGVPLPTPY
DLRKKILIKNKKMHGLTDEEKKKIEKEKKDAGTAAKEAEAAEEMSALVNY
IQPVHFTTFEQAQKKDRHYEMSSMVETQALNKLKDNPEDFVDYNKKQITR
IYPKGTRVDSSNYVPQIYWNAGCQLVALNFQCFDIAMCVNLGVFEYNGCS
GYLLKPEFMRKLDKRFDPFTESTVDGVVAGTIEIKIISAQFLSDKQISSY
VEVEMYGLPTDTVRKKFKTKIIENNGMDPYYDEKVFVFKKVVLPDLAVVR
IIVSEENGKFIGHRVMPLDGIKPGYRHVPLRNESNRPLGLASVFAHIVAK
DYVSYQSAQEARAAALCAFEDDPDAALNAAK
3D structure
PDB3qr0 An autoinhibitory helix in the C-terminal region of phospholipase C-beta mediates Galphaq activation.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H338 N339 E368 D370 H383 E417
Catalytic site (residue number reindexed from 1) H328 N329 E358 D360 H373 E407
Enzyme Commision number 3.1.4.11: phosphoinositide phospholipase C.
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 CA A N339 E368 D370 E417 N329 E358 D360 E407
Gene Ontology
Molecular Function
GO:0004435 phosphatidylinositol phospholipase C activity
GO:0008081 phosphoric diester hydrolase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0007165 signal transduction
GO:0035556 intracellular signal transduction

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3qr0, PDBe:3qr0, PDBj:3qr0
PDBsum3qr0
PubMed21822282
UniProtF2YQ19

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