Structure of PDB 5m12 Chain A

Receptor sequence
>5m12A (length=534) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VPRGSHMASMEIFGKTFREGRFVLKEKNFTVEFAVEKIHLGWKISGRVKG
SPGRLEVLRTKAPEKVLVNNWQSWGPCRVVDAFSFKPPEIDPNWRYTASV
VPDVLERNLQSDYFVAEEGKVYGFLSSKIAHPFFAVEDGELVAYLEYFDV
EFDDFVPLEPLVVLEDPNTPLLLEKYAELVGMENNARVPKHTPTGWCSWY
HYFLDLTWEETLKNLKLAKNFPFEVFQIDDAYEKDIGDWLVTRGDFPSVE
EMAKVIAENGFIPGIWTAPFSVSETSDVFNEHPDWVVKENGEPKMAYRNW
NKKIYALDLSKDEVLNWLFDLFSSLRKMGYRYFKIDFLFAGAVPGERKKN
ITPIQAFRKGIETIRKAVGEDSFILGCGSPLLPAVGCVDGMRIGPDTAPF
WGEHIEDNGAPAARWALRNAITRYFMHDRFWLNDPDCLILREEKTDLTQK
EKELYSYTCGVLDNMIIESDDLSLVRDHGKKVLKETLELLGGRPRVQNIM
SEDLRYEIVSSGTLSGNVKIVVDLNSREYHLEKE
3D structure
PDB5m12 Structural Snapshots for Mechanism-Based Inactivation of a Glycoside Hydrolase by Cyclopropyl Carbasugars.
ChainA
Resolution1.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V26
Catalytic site (residue number reindexed from 1) V35
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 D428 D463
BS02 7D0 A W65 W85 W190 Y191 D220 D221 W257 N290 K325 D327 F328 C368 R383 D387 W74 W94 W199 Y200 D229 D230 W266 N299 K334 D336 F337 C377 R392 D396
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5m12, PDBe:5m12, PDBj:5m12
PDBsum5m12
PubMed27783466
UniProtG4FEF4|AGAL_THEMA Alpha-galactosidase (Gene Name=galA)

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