Structure of PDB 3a23 Chain B

Receptor sequence
>3a23B (length=612) Species: 33903 (Streptomyces avermitilis) [Search protein sequence]
TTRQITVPSAPMGWASWNSFAAKIDYSVIKKQVDAFVAAGLPAAGYTYIN
IDEGWWQGTRDSAGNITVDTAEWPGGMSAITAYIHSKGLKAGIYTDAGKD
GCGYYYPTGRPAAPGSGSEGHYDQDMLQFSTWGFDFVKVDWCGGDAEGLD
AATTYKSISDAVGRAAATTGRPLTLSICNWGYQNPWNWAAGQAPLWRTST
DIIYYGNQPSMTSLLSNFDQTLHPTAQHTGYYNDPDMLMVGMDGFTAAQN
RTHMNLWAISGAPLLAGNDLTTMTSETAGILKNPEVIAVDQDSRGLQGVK
VAEDTTGLQAYGKVLSGTGNRAVVLLNRTSAAHDITVRWSDLGLTNASAT
VRDLWARQNVGTSATGYTASVPAGGSVMLTVTGGTEAAGGAYAATSTGRY
TGVTAASTGLNVVDVAYTNNTSSARTATLQVNGQTATTVSFPPTGASAGT
VSVEVSLSKGSANTLALSGGPATEGITVRPLPGTNGALVTGKQSGRCADI
YNNTITNGTQAELWDCNGGPNQSWTYTSRKELVLYGNKCLDAYNLGTTNG
TKVVIWDCNGQANQKWNINSDGTITNVNAGLCLDAYNAATANGTSLVLWS
CGTGDNQKWTVT
3D structure
PDB3a23 A beta-l-Arabinopyranosidase from Streptomyces avermitilis is a novel member of glycoside hydrolase family 27.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D186 D247
Catalytic site (residue number reindexed from 1) D140 D201
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 GAL B W63 D98 E99 Y140 C148 K184 D186 C224 W226 R243 D247 W17 D52 E53 Y94 C102 K138 D140 C178 W180 R197 D201 MOAD: Ka=610M^-1
BS02 GAL B D630 Y632 N633 W645 N652 D584 Y586 N587 W599 N606 MOAD: Ka=610M^-1
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3a23, PDBe:3a23, PDBj:3a23
PDBsum3a23
PubMed19608743
UniProtQ82L26

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