Structure of PDB 1t0o Chain A

Receptor sequence
>1t0oA (length=417) Species: 51453 (Trichoderma reesei) [Search protein sequence]
IVMPDGVTGKVPSLGWNSWNAYHCDIDESKFLSAAELIVSSGLLDAGYNY
VNIDDCWSMKDGRVDGHIAPNATRFPDGIDGLAKKVHALGLKLGIYSTAG
TATCAGYPASLGYEDVDAADFADWGVDYLKYDNCNVPSDWQDEYVACNPD
FVKTGPNGTCTTALDPTLAPPGYDWSTSKSAERFGAMRNALAKQSHEIVL
SMCIWGQADVFSWGNSTGISWRMSDDISPNWGSVTRILNLNSFKLNSVDF
WGHNDADMLEVGNGNLTAAETRTHFALWAAMKSPLLIGTDLAQLSQNNIN
LLKNKHLLAFNQDSVYGQPATPYKWGINPDWTFNVTYPAEFWAGPSSKGH
LVLMVNTLDITATKEAKWNEIPGLSAGHYEVRDVWSDKDLGCLSSYKAAV
AAHDTAVILVGKKCQRW
3D structure
PDB1t0o Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism
ChainA
Resolution1.96 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D132 D226
Catalytic site (residue number reindexed from 1) D132 D226
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 MAN A S242 F243 L245 T321 P322 W331 S242 F243 L245 T321 P322 W331
BS02 GAL A W19 D54 D55 C104 K130 D132 C203 W205 R222 D226 W19 D54 D55 C104 K130 D132 C203 W205 R222 D226
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004557 alpha-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009311 oligosaccharide metabolic process
GO:0016139 glycoside catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1t0o, PDBe:1t0o, PDBj:1t0o
PDBsum1t0o
PubMed15136043
UniProtQ92456

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