Structure of PDB 5epc Chain A

Receptor sequence
>5epcA (length=561) Species: 9606 (Homo sapiens) [Search protein sequence]
SNMVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVE
PAQRQEATLVVGGDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPA
VSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIF
QISKTIEEYAVCPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATM
LRSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSA
VNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILG
KHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVASAT
KIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAW
LSILATRKQSVEDILKDHWQKYGRNFFTRYDYEEVEAEGANKMMKDLEAL
MFDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISRNQGLRLIFTDGS
RIVFRLSGAGATIRLYIDSYEKDVAKINQDPQVMLAPLISIALKVSQLQE
RTGRTAPTVIT
3D structure
PDB5epc Induced Structural Disorder as a Molecular Mechanism for Enzyme Dysfunction in Phosphoglucomutase 1 Deficiency.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R23 S117 H118 K130 D288 D290 D292 R293 G380 K389
Catalytic site (residue number reindexed from 1) R25 S119 H120 K132 D290 D292 D294 R295 G382 K391
Enzyme Commision number 5.4.2.2: phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
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 MG A S117 D288 D290 D292 S119 D290 D292 D294
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004614 phosphoglucomutase activity
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0016868 intramolecular phosphotransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006006 glucose metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome
GO:1904724 tertiary granule lumen
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:5epc, PDBe:5epc, PDBj:5epc
PDBsum5epc
PubMed26972339
UniProtP36871|PGM1_HUMAN Phosphoglucomutase-1 (Gene Name=PGM1)

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