Structure of PDB 1mw0 Chain A

Receptor sequence
>1mw0A (length=628) Species: 489 (Neisseria polysaccharea) [Search protein sequence]
SPNSQYLKTRILDIYTPEQRAGIEKSEDWRQFSRRMDTHFPKLMNELDSV
YGNNEALLPMLEMLLAQAWQSYSQRNSSLKDIDIARENNPDWILSNKQVG
GVCYVDLFAGDLKGLKDKIPYFQELGLTYLYLMPLFKCPEGKSDGGYAVS
SYRDVNPALGTIGDLREVIAALHEAGISAVVDFIFNHTSNEHEWAQRCAA
GDPLFDNFYYIFPDRRMPDQYDRTLREIFPDQHPGGFSQLEDGRWVWTTF
NSFQWDLNYSNPWVFRAMAGEMLFLANLGVDILRMDAVAFIWKQMGTSCE
NLPQAHALIRAFNAVMRIAAPAVFFKSQAIVHPDQVVQYIGQDECQIGYN
PLQMALLWNTLATREVNLLHQALTYRHNLPEHTAWVNYVRSHDDIGWTFA
DEDAAYLGISGYDHRQFLNRFFVNRFDGSFARGVPFQYNPSTGDCRVSGT
AAALVGLAQDDPHAVDRIKLLYSIALSTGGLPLIYLGDEVGTLNDDDWSQ
DSNKSDDSRWAHRPRYNEALYAQRNDPSTAAGQIYQGLRHMIAVRQSNPR
FDGGRLVTFNTNNKHIIGYIRNNALLAFGNFSEYPQTVTAHTLQAMPFKA
HDLIGGKTVSLNQDLTLQPYQVMWLEIA
3D structure
PDB1mw0 Oligosaccharide and Sucrose Complexes of Amylosucrase. STRUCTURAL IMPLICATIONS FOR THE POLYMERASE ACTIVITY
ChainA
Resolution2.01 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D182 R284 D286 Q328 H392 D393
Catalytic site (residue number reindexed from 1) D182 R284 D286 Q328 H392 D393
Enzyme Commision number 2.4.1.4: amylosucrase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
GO:0047669 amylosucrase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1mw0, PDBe:1mw0, PDBj:1mw0
PDBsum1mw0
PubMed12364331
UniProtQ9ZEU2|AMYS_NEIPO Amylosucrase (Gene Name=ams)

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