Structure of PDB 1so0 Chain D

Receptor sequence
>1so0D (length=342) Species: 9606 (Homo sapiens) [Search protein sequence]
MASVTRAVFGELPSGGGTVEKFQLQSDLLRVDIISWGCTITALEVKDRQG
RASDVVLGFAELEGYLQKQPYFGAVIGRVANRIAKGTFKVDGKEYHLAIN
KEPNSLHGGVRGFDKVLWTPRVLSNGVQFSRISPDGEEGYPGELKVWVTY
TLDGGELIVNYRAQASQATPVNLTNHSYFNLAGQASPNINDHEVTIEADT
YLPVDETLIPTGEVAPVQGTAFDLRKPVELGKHLQDFHLNGFDHNFCLKG
SKEKHFCARVHHAASGRVLEVYTTQPGVQFYTGNFLDGTLKGKNGAVYPK
HSGFCLETQNWPDAVNQPRFPPVLLRPGEEYDHTTWFKFSVA
3D structure
PDB1so0 Molecular structure of human galactose mutarotase
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H107 H176 E307
Catalytic site (residue number reindexed from 1) H107 H176 E307
Enzyme Commision number 5.1.3.3: aldose 1-epimerase.
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 GAL D R82 H107 H176 D243 E307 R82 H107 H176 D243 E307
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004034 aldose 1-epimerase activity
GO:0016853 isomerase activity
GO:0030246 carbohydrate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006006 glucose metabolic process
GO:0006012 galactose metabolic process
GO:0019318 hexose metabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005737 cytoplasm
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1so0, PDBe:1so0, PDBj:1so0
PDBsum1so0
PubMed15026423
UniProtQ96C23|GALM_HUMAN Galactose mutarotase (Gene Name=GALM)

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