Structure of PDB 7gpb Chain B

Receptor sequence
>7gpbB (length=823) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
RKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACD
EATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGI
RYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHT
SQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNV
GGYIQAVLDRNLAENISRVLYPEGKELRLKQEYFVVAATLQDIIRRFKSS
KFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKA
WEVTVKTCAYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRFLNRV
AAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILK
KTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISD
LDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFD
VQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYH
MAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSE
QISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMR
VEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNM
LMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSD
RTIAQYAREIWGVEPSRQRLPAP
3D structure
PDB7gpb Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP.
ChainB
Resolution2.9 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) H377 K568 R569 K574 T676 K680
Catalytic site (residue number reindexed from 1) H363 K554 R555 K560 T662 K666
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 K568 Y648 R649 G675 G677 K680 K554 Y634 R635 G661 G663 K666
BS02 AMP B Q71 Y75 R309 R310 Q62 Y66 R295 R296 PDBbind-CN: -logKd/Ki=5.52,Kd=3uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0005977 glycogen metabolic process
GO:0005980 glycogen catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0098723 skeletal muscle myofibril

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7gpb, PDBe:7gpb, PDBj:7gpb
PDBsum7gpb
PubMed1900534
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

[Back to BioLiP]