Structure of PDB 3czg Chain A

Receptor sequence
>3czgA (length=607) [Search protein sequence]
IDPPALRAAFAGPLDPQHAEVLLSRYDQHASRLLDALHALYGQRADYASW
LAQWLGEVGDIARQRPQALQTLDSTRHAGWFGQPHMLGYSAYADRFAGTL
QGVAERVPYLQELGVRYLHLLPFLRARAGDNDGGFAVSDYGQVEPSLGSN
DDLVALTSRLREAGISLCADFVLNHTADDHAWAQAARAGDARYLDYYHHF
ADRTVPDRYEATLGQVGNFTWVDDTAQWMWTTFYPYQWDLNWSNPAVFGD
MALAMLRLANLGVEAFRLDSTAYLWKRIGTDCMNQSEAHTLLVALRAVTD
IVAPAVVMKAEAIVPMTQLPPYFGSGVDEGHECHLAYHSTLMAAGWSALA
LQRGDILHNVIAHSPPLPRHCAWLSYVRCHDDIGWNVLQHEACGNAAQPP
FSLRDVARFYANAVPGSYARGESFGVHGTNGMAAALAGIQAAQEAGDAAA
LAVAVDRLVLLYAIALAMPGVPLIYMGDELAMVNDPGYRDDPHRQHEGRW
LHRPAMDWQLAAQRHDAKSLSGTVYRRLRGLIRQRAALGALAADQALASI
ALNDPRVFALTRGDSFIALHNFSDQLLDVELAAIGVDGWTLLSIVLPPYG
VRWLQRG
3D structure
PDB3czg Crystal structures and mutagenesis of sucrose hydrolase from Xanthomonas axonopodis pv. glycines: insight into the exclusively hydrolytic amylosucrase fold.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D175 D280 E322 H391 D392
Catalytic site (residue number reindexed from 1) D170 D269 E311 H380 D381
Enzyme Commision number 3.2.1.48: sucrose alpha-glucosidase.
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 GLC A D137 F140 F244 H391 D392 R515 D132 F135 F233 H380 D381 R499
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0047669 amylosucrase activity
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3czg, PDBe:3czg, PDBj:3czg
PDBsum3czg
PubMed18565544
UniProtQ6UVM5

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