Structure of PDB 3a22 Chain A

Receptor sequence
>3a22A (length=614) Species: 33903 (Streptomyces avermitilis) [Search protein sequence]
AVTTRQITVPSAPMGWASWNSFAAKIDYSVIKKQVDAFVAAGLPAAGYTY
INIDEGWWQGTRDSAGNITVDTAEWPGGMSAITAYIHSKGLKAGIYTDAG
KDGCGYYYPTGRPAAPGSGSEGHYDQDMLQFSTWGFDFVKVDWCGGDAEG
LDAATTYKSISDAVGRAAATTGRPLTLSICNWGYQNPWNWAAGQAPLWRT
STDIIYYGNQPSMTSLLSNFDQTLHPTAQHTGYYNDPDMLMVGMDGFTAA
QNRTHMNLWAISGAPLLAGNDLTTMTSETAGILKNPEVIAVDQDSRGLQG
VKVAEDTTGLQAYGKVLSGTGNRAVVLLNRTSAAHDITVRWSDLGLTNAS
ATVRDLWARQNVGTSATGYTASVPAGGSVMLTVTGGTEAAGGAYAATSTG
RYTGVTAASTGLNVVDVAYTNNTSSARTATLQVNGQTATTVSFPPTGASA
GTVSVEVSLSKGSANTLALSGGPATEGITVRPLPGTNGALVTGKQSGRCA
DIYNNTITNGTQAELWDCNGGPNQSWTYTSRKELVLYGNKCLDAYNLGTT
NGTKVVIWDCNGQANQKWNINSDGTITNVNAGLCLDAYNAATANGTSLVL
WSCGTGDNQKWTVT
3D structure
PDB3a22 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 ARA A W63 D98 Y140 K184 D186 C224 R243 D247 W19 D54 Y96 K140 D142 C180 R199 D203 MOAD: Ka=150M^-1
BS02 ARA A D545 Y547 N548 W560 N563 N567 D501 Y503 N504 W516 N519 N523 MOAD: Ka=150M^-1
BS03 ARA A D587 Y589 N590 W602 N605 Q607 N609 D543 Y545 N546 W558 N561 Q563 N565 MOAD: Ka=150M^-1
BS04 ARA A D630 Y632 N633 W645 N652 D586 Y588 N589 W601 N608 MOAD: Ka=150M^-1
BS05 ARA A Y547 E558 Y503 E514 MOAD: Ka=150M^-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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3a22, PDBe:3a22, PDBj:3a22
PDBsum3a22
PubMed19608743
UniProtQ82L26

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