Structure of PDB 6gx8 Chain A

Receptor sequence
>6gx8A (length=534) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
VPRGSHMASMEIFGKTFREGRFVLKEKNFTVEFAVEKIHLGWKISGRVKG
SPGRLEVLRTKAPEKVLVNNWQSWGPCRVVDAFSFKPPEIDPNWRYTASV
VPDVLERNLQSDYFVAEEGKVYGFLSSKIAHPFFAVEDGELVAYLEYFDV
EFDDFVPLEPLVVLEDPNTPLLLEKYAELVGMENNARVPKHTPTGWCSWY
HYFLDLTWEETLKNLKLAKNFPFEVFQIDDAYEKDIGDWLVTRGDFPSVE
EMAKVIAENGFIPGIWTAPFSVSETSDVFNEHPDWVVKENGEPKMAYRNW
NKKIYALDLSKDEVLNWLFDLFSSLRKMGYRYFKIDFLFAGAVPGERKKN
ITPIQAFRKGIETIRKAVGEDSFILGCGSPLLPAVGCVDGMRIGPDTAPF
WGEHIEDNGAPAARWALRNAITRYFMHDRFWLNDPDCLILREEKTDLTQK
EKELYSYTCGVLDNMIIESDDLSLVRDHGKKVLKETLELLGGRPRVQNIM
SEDLRYEIVSSGTLSGNVKIVVDLNSREYHLEKE
3D structure
PDB6gx8 Revealing the mechanism for covalent inhibition of glycoside hydrolases by carbasugars at an atomic level.
ChainA
Resolution1.42 Å
3D
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
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 FH2 A W65 W190 Y191 D220 D221 W257 K325 D327 F328 C368 R383 D387 W74 W199 Y200 D229 D230 W266 K334 D336 F337 C377 R392 D396
BS02 MG A D419 D454 D428 D463
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:6gx8, PDBe:6gx8, PDBj:6gx8
PDBsum6gx8
PubMed30104598
UniProtG4FEF4|AGAL_THEMA Alpha-galactosidase (Gene Name=galA)

[Back to BioLiP]