Structure of PDB 3a23 Chain A

Receptor sequence
>3a23A (length=614) Species: 33903 (Streptomyces avermitilis) [Search protein sequence]
AVTTRQITVPSAPMGWASWNSFAAKIDYSVIKKQVDAFVAAGLPAAGYTY
INIDEGWWQGTRDSAGNITVDTAEWPGGMSAITAYIHSKGLKAGIYTDAG
KDGCGYYYPTGRPAAPGSGSEGHYDQDMLQFSTWGFDFVKVDWCGGDAEG
LDAATTYKSISDAVGRAAATTGRPLTLSICNWGYQNPWNWAAGQAPLWRT
STDIIYYGNQPSMTSLLSNFDQTLHPTAQHTGYYNDPDMLMVGMDGFTAA
QNRTHMNLWAISGAPLLAGNDLTTMTSETAGILKNPEVIAVDQDSRGLQG
VKVAEDTTGLQAYGKVLSGTGNRAVVLLNRTSAAHDITVRWSDLGLTNAS
ATVRDLWARQNVGTSATGYTASVPAGGSVMLTVTGGTEAAGGAYAATSTG
RYTGVTAASTGLNVVDVAYTNNTSSARTATLQVNGQTATTVSFPPTGASA
GTVSVEVSLSKGSANTLALSGGPATEGITVRPLPGTNGALVTGKQSGRCA
DIYNNTITNGTQAELWDCNGGPNQSWTYTSRKELVLYGNKCLDAYNLGTT
NGTKVVIWDCNGQANQKWNINSDGTITNVNAGLCLDAYNAATANGTSLVL
WSCGTGDNQKWTVT
3D structure
PDB3a23 A beta-l-Arabinopyranosidase from Streptomyces avermitilis is a novel member of glycoside hydrolase family 27.
ChainA
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) D142 D203
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 A W63 D98 E99 Y140 C148 K184 D186 C224 R243 D247 W19 D54 E55 Y96 C104 K140 D142 C180 R199 D203 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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