Structure of PDB 5tr2 Chain A

Receptor sequence
>5tr2A (length=561) Species: 9606 (Homo sapiens) [Search protein sequence]
NMVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEP
AQRQEATLVVGGDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPAV
SCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQ
ISKTIEEYAVCPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATML
RSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAV
NCVPLEDFGGHHPGPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGK
HGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVASATK
IALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWL
SILATRKQSVEDILKDHWQKYGRNFFTRYDYEEVEAEGANKMMKDLEALM
FDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISRNQGLRLIFTDGSR
IVFRLSGTAGATIRLYIDSYEKDVAKINQDPQVMLAPLISIALKVSQLQE
RTGRTAPTVIT
3D structure
PDB5tr2 Asp263 missense variants perturb the active site of human phosphoglucomutase 1.
ChainA
Resolution2.5 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) R24 S118 H119 K131 D289 D291 D293 R294 G381 K390
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 CA A S117 D288 D290 D292 S118 D289 D291 D293
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:5tr2, PDBe:5tr2, PDBj:5tr2
PDBsum5tr2
PubMed28117557
UniProtP36871|PGM1_HUMAN Phosphoglucomutase-1 (Gene Name=PGM1)

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