Structure of PDB 5lrb Chain B

Receptor sequence
>5lrbB (length=843) Species: 112509 (Hordeum vulgare subsp. vulgare) [Search protein sequence]
IDSSAIASNIQHHADFTPLFSPEHSSPLKAYHATAKSVFDSLIMNWNATY
DYYNKVNAKQAYYLSMEFLQGRALTNAIGNLELTGQYAEALKQLGHNLED
VASQEPDPALGNGGLGRLASCFLDSLATLNYPAWGYGLRYRYGLFKQIIT
KDGQEEVAENWLEMGNPWEIVRNDVSYPVKFYGKVVEGTDGRKHWIGGEN
IKAVAHDVPIPGYKTKTTNNLRLWSTTVPSQNFDLGAFNAGDHAKANEAH
LNAEKICHVLYPGDESSEGKILRLKQQYTLCSASLQDIISRFESRAGDSL
NWEDFPSKVAVQMNDTHPTLCIPELMRILMDIKGLSWNEAWSITERTVAY
TNHTVLPEALEKWSLDIMQKLLPRHVEIIETIDEELMNNIVSKYGTADIS
LLKQKLKDMRILDNVDLPASVAKLFIKELDPFAKYDPQFPRVVRMANLCV
VGGHSVNGVAEIHSEIVKQDVFNSFYEMWPTKFQNKTNGVTPRRWIRFCN
PELSTIISKWIGSDDWILNTDKLAGLKKFADDEDLQSEWRTAKRNNKMKV
VSLIRDKTGYIVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMSA
KDRRKSFVPRVCIFGGKAFATYVQAKRIVKFITDVAATVNYDPDIGDLLK
VVFVPDYNVSVAETLIPASELSQHISTAGMEASGTSNMKFAMNGCLLIGT
LDGANVEIREEVGEENFFLFGAHAPEIAGLRQERAEGKFVPDLRFEEVKE
YVRSGVFGTSNYDELMGSLEGNEGYGRADYFLVGKDFPSYIECQEKVDEA
YRDQKLWTRMSILNTAGSPKFSSDRTIHEYAKDIWDISPVIMP
3D structure
PDB5lrb Functional and structural characterization of plastidic starch phosphorylase during barley endosperm development.
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H421 K698 R699 K704 T810 K814
Catalytic site (residue number reindexed from 1) H353 K573 R574 K579 T685 K689
Enzyme Commision number 2.4.1.1: glycogen phosphorylase.
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 GLC B M967 P968 M842 P843
BS02 AC1 B E702 Y747 E577 Y622
BS03 GLC B H421 R699 S808 G809 H353 R574 S683 G684
BS04 PLP B L137 W620 Y782 N783 V784 T810 S811 K814 L69 W495 Y657 N658 V659 T685 S686 K689
Gene Ontology
Molecular Function
GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
GO:0008184 glycogen phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009266 response to temperature stimulus
GO:0009414 response to water deprivation

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Molecular Function
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Biological Process
External links
PDB RCSB:5lrb, PDBe:5lrb, PDBj:5lrb
PDBsum5lrb
PubMed28407006
UniProtF2E0G2

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