Structure of PDB 1fc0 Chain B

Receptor sequence
>1fc0B (length=793) Species: 9606 (Homo sapiens) [Search protein sequence]
NVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQ
HYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEEL
EEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRD
GWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVL
ALPYDTPVPGYMNNTVNTMRLWSARAPGDYIQAVLDRNLAENISRVLYPN
DNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFGTVFDAFPDQVAIQLN
DTHPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALERWP
VDLVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEGSKR
INMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNGITP
RRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVK
QENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYN
RIKKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGS
KLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALT
IGTMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEALPEL
KLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQDKVS
QLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSD
3D structure
PDB1fc0 Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H1377 K1568 R1569 K1574 T1676 K1680
Catalytic site (residue number reindexed from 1) H339 K530 R531 K536 T638 K642
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 NBG B G1135 L1136 N1284 H1377 T1378 N1484 E1672 A1673 S1674 G1675 G113 L114 N252 H339 T340 N446 E634 A635 S636 G637
BS02 PLP B G1134 K1568 Y1648 R1649 V1650 G1675 T1676 K1680 G112 K530 Y610 R611 V612 G637 T638 K642
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0002060 purine nucleobase binding
GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0005536 D-glucose binding
GO:0008184 glycogen phosphorylase activity
GO:0016208 AMP binding
GO:0016757 glycosyltransferase activity
GO:0019842 vitamin binding
GO:0030170 pyridoxal phosphate binding
GO:0030246 carbohydrate binding
GO:0032052 bile acid binding
GO:0042802 identical protein binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005977 glycogen metabolic process
GO:0005980 glycogen catabolic process
GO:0006015 5-phosphoribose 1-diphosphate biosynthetic process
GO:0009617 response to bacterium
GO:0042593 glucose homeostasis
GO:0070266 necroptotic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fc0, PDBe:1fc0, PDBj:1fc0
PDBsum1fc0
PubMed10949035
UniProtP06737|PYGL_HUMAN Glycogen phosphorylase, liver form (Gene Name=PYGL)

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