Structure of PDB 4bqi Chain B

Receptor sequence
>4bqiB (length=824) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
KISAKANPEADDATEIAGNIVYHAKYSPHFSPLKFGPEQALYATAESLRD
RLIQLWNETYVHFNKVDPKQTYYLSMEYLQGRALTNAIGNLNLQGPYADA
LRTLGYELEEIAEQEKDAALGNGGLGRLASCFLDSMATLNLPAWGYGLRY
RHGLFKQIITKKGQEEIPEDWLEKFSPWEIVRHDVVFPVRFFGKVQVNPD
GSRKWVDGDVVQALAYDVPIPGYGTKNTISLRLWEAKARAEDLDLFQFNE
GEYELAAQLHSRAQQICTVLYPGDATENGKLLRLKQQFFLCSASLQDIIS
RFHERSTTRKWSEFPSKVAVQMNDTHPTLAIPELMRLLMDDNGLGWDEAW
DVTSKTVAYTNHTVLPEALEKWSQSLMWKLLPRHMEIIEEIDKRFVQTIR
DTRVDLEDKISSLSILDNNPQKPVVRMANLCVVSSHTVNGVAQLHSDILK
AELFADYVSIWPNKFQNKTNGITPRRWLRFCSPELSDIITKWLKTDKWIT
DLDLLTGLRQFADNEELQSEWASAKTANKKRLAQYIERVTGVSIDPTSLF
DIQVKRIHEYKRQLMNILGVVYRFKKLKEMKPEERKKTVPRTVMIGGKAF
ATYTNAKRIVKLVNDVGDVVNSDPEVNEYLKVVFVPNYNVTVAEMLIPGS
ELSQHISTAGMEASGTSNMKFALNGCLIIGTLDGANVEIREEVGEENFFL
FGATADQVPRLRKEREDGLFKPDPRFEEAKQFVKSGVFGSYDYGPLLDSL
EGNTGFGRGDYFLVGYDFPSYMDAQAKVDEAYKDRKGWLKMSILSTAGSG
KFSSDRTIAQYAKEIWNIEACPVP
3D structure
PDB4bqi Sugar-Coated Sensor Chip and Nanoparticle Surfaces for the in Vitro Enzymatic Synthesis of Starch-Like Materials
ChainB
Resolution1.9 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) H379 K572 R573 K578 T683 K687
Catalytic site (residue number reindexed from 1) H362 K555 R556 K561 T666 K670
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 R217 R400 E407 R203 R383 E390
BS02 GLC B G362 W363 G345 W346
BS03 PLP B L93 W494 Y655 N656 V657 G682 S684 K687 L79 W477 Y638 N639 V640 G665 S667 K670
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:0009414 response to water deprivation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009507 chloroplast

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4bqi, PDBe:4bqi, PDBj:4bqi
PDBsum4bqi
PubMed
UniProtQ9SD76|PHS2_ARATH Alpha-glucan phosphorylase 2, cytosolic (Gene Name=PHS2)

[Back to BioLiP]