Structure of PDB 2c4m Chain B

Receptor sequence
>2c4mB (length=788) Species: 1721 (Corynebacterium callunae) [Search protein sequence]
PLPAALVGSHVRAAAGTPADLATDRKFWTGLSRAVQERIADDWERTREAY
GAARQQHYFSAEFLMGRALLNNLTNLGLVDEAAAATRELGHELTDILEIE
NDAALGNGGLGRLAACFLDSAVTQDYPVTGYGLLYRFGLFRQSFNEGFQV
EKPDPWREEEYPFTIRRASDQLVVCFDDMKTRAIPYDMPITGYGTHNVGT
LRLWKAEPWEEFDYDAFNAQRFTDAIIERERVSDICRVLYPNDTTYEGKK
LRVRQQYFFTSASLQAMIQDHLAHHKDLSNFAEFHSVQLNDTHPVLAIPE
LMRLLMDEHDMGWEESWAIVSKTFAYTNHTVLTEALEQWDEQIFQQLFWR
VWEIIAEIDRRFRLERAADGLDEETINRMAPIQHGTVHMAWIACYAAYSI
NGVAALHTEIIKAETLADWYALWPEKFNNKTNGVTPRRWLRMINPGLSDL
LTRLSGSDDWVTDLDELKKLRSYADDKSVLEELRAIKAANKQDFAEWILE
RQGIEIDPESIFDVQIKRLHEYKRQLMNALYVLDLYFRIKEDGLTDIPAR
TVIFGAKAAPGYVRAKAIIKLINSIADLVNNDPEVSPLLKVVFVENYNVS
PAEHILPASDVSEQISTAGKEASGTSNMKFMMNGALTLGTMDGANVEIVD
SVGEENAYIFGARVEELPALRESYKPYELYETVPGLKRALDALDNGTLND
NNSGLFYDLKHSLIHGYGKDASDTYYVLGDFADYRETRDRMAADYASDPL
GWARMAWINICESGRFSSDRTIRDYATEIWKLEPTPAV
3D structure
PDB2c4m Starch Phosphorylase: Structural Studies Explain Oxyanion-Dependent Kinetic Stability and Regulatory Control
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) H334 K522 R523 K528 T630 K634
Catalytic site (residue number reindexed from 1) H329 K517 R518 K523 T625 K629
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 PLP B L69 G114 W444 K522 N603 V604 T630 S631 K634 L64 G109 W439 K517 N598 V599 T625 S626 K629
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:0005980 glycogen catabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2c4m, PDBe:2c4m, PDBj:2c4m
PDBsum2c4m
PubMed
UniProtQ8KQ56

[Back to BioLiP]