Structure of PDB 6sno Chain A Binding Site BS01

Receptor Information
>6sno Chain A (length=573) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EWISGTYRKMEEGPLPLLTFATAPYHDQKPGTSGLRKKTYYFEEKPCYLE
NFIQSIFFSIDLKDRQGSSLVVGGDGRYFNKSAIETIVQMAAANGIGRLV
IGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGG
PAPEAITDKIFQISKTIEEYAVCPDLKVDLGVLGKQQFDLENKFKPFTVE
IVDSVEAYATMLRSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKIL
CEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAF
DGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPT
SGALDRVASATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIR
EKDGLWAVLAWLSILATRKQSVEDILKDHWQKYGRNFFTRYDYEEVEAEG
ANKMMKDLEALMFDRSFVGKQFSANVYTVEKADNFEYSDPVDGSISRNQG
LRLIFTDGSRIVFRLSGTGSAGATIRLYIDSYEKDVAKINQDPQVMLAPL
ISIALKVSQLQERTGRTAPTVIT
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain6sno Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6sno Structural basis for substrate and product recognition in human phosphoglucomutase-1 (PGM1) isoform 2, a member of the alpha-D-phosphohexomutase superfamily.
Resolution2.7 Å
Binding residue
(original residue number in PDB)
S135 D306 D308 D310
Binding residue
(residue number reindexed from 1)
S130 D301 D303 D305
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R41 S135 H136 K148 D306 D308 D310 R311 G398
Catalytic site (residue number reindexed from 1) R36 S130 H131 K143 D301 D303 D305 R306 G393
Enzyme Commision number 5.4.2.2: phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
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:6sno, PDBe:6sno, PDBj:6sno
PDBsum6sno
PubMed32221390
UniProtP36871|PGM1_HUMAN Phosphoglucomutase-1 (Gene Name=PGM1)

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