Structure of PDB 5m0x Chain A

Receptor sequence
>5m0xA (length=533) Species: 2336 (Thermotoga maritima) [Search protein sequence]
PRGSHMASMEIFGKTFREGRFVLKEKNFTVEFAVEKIHLGWKISGRVKGS
PGRLEVLRTKAPEKVLVNNWQSWGPCRVVDAFSFKPPEIDPNWRYTASVV
PDVLERNLQSDYFVAEEGKVYGFLSSKIAHPFFAVEDGELVAYLEYFDVE
FDDFVPLEPLVVLEDPNTPLLLEKYAELVGMENNARVPKHTPTGWCSWYH
YFLDLTWEETLKNLKLAKNFPFEVFQIDDAYEKDIGDWLVTRGDFPSVEE
MAKVIAENGFIPGIWTAPFSVSETSDVFNEHPDWVVKENGEPKMAYRNWN
KKIYALDLSKDEVLNWLFDLFSSLRKMGYRYFKIDFLFAGAVPGERKKNI
TPIQAFRKGIETIRKAVGEDSFILGCGSPLLPAVGCVDGMRIGPDTAPFW
GEHIEDNGAPAARWALRNAITRYFMHDRFWLNDPDCLILREEKTDLTQKE
KELYSYTCGVLDNMIIESDDLSLVRDHGKKVLKETLELLGGRPRVQNIMS
EDLRYEIVSSGTLSGNVKIVVDLNSREYHLEKE
3D structure
PDB5m0x Structural Snapshots for Mechanism-Based Inactivation of a Glycoside Hydrolase by Cyclopropyl Carbasugars.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) V26
Catalytic site (residue number reindexed from 1) V34
Enzyme Commision number 3.2.1.22: alpha-galactosidase.
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 D419 D454 D427 D462
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004557 alpha-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016139 glycoside catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5m0x, PDBe:5m0x, PDBj:5m0x
PDBsum5m0x
PubMed27783466
UniProtG4FEF4|AGAL_THEMA Alpha-galactosidase (Gene Name=galA)

[Back to BioLiP]