Structure of PDB 6m6t Chain E

Receptor sequence
>6m6tE (length=497) Species: 1311 (Streptococcus agalactiae) [Search protein sequence]
KRASGVLMHITSLPGDLGIGTFGREAYAFVDFLVETDQKFWQILPLTTTS
FGDSPYQSFSAVAGNTHLIDFDLLTLEGFISKDDYQNISFGQDPEVVDYA
GLFEKRRPVLEKAVKNFLKEERATRMLSDFLQEEKWVTDFAEFMAIKEHF
GNKALQEWDDKAIIRREEEALAGYRQKLSEVIKYHEVTQYFFYKQWFELK
EYANDKGIQIIGDMPIYVSADSVEVWTMPELFKLDRDKQPLAIAGVPADD
FSDDGQLWGNPIYNWDYHKESDFDWWIYRIQSGVKMYDYLRIDHFKGFSD
YWEIRGDYQTANDGSWQPAPGPELFATIKEKLGDLPIIAENLGYIDERAE
RLLAGTGFPGMKIMEFGFYDTTGNSIDIPHNYTENTIAYAGTHDNEVING
WFENLTVEQKAYAENYMRRLPNEPITETVLRTLYATVSQTTITCMQDLLD
KPADSRMNMPNTVGGNWQWRMRKEDLTENRKAFLKEITTIYNRGNKL
3D structure
PDB6m6t Streptococcus agalactiae amylomaltase offers insight into the transglycosylation mechanism and the molecular basis of thermostability among amylomaltases.
ChainE
Resolution2.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.25: 4-alpha-glucanotransferase.
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 ASO E Y58 W260 D295 D396 Y56 W258 D293 D394
BS02 AC1 E S56 L259 P462 N463 S54 L257 P460 N461
BS03 GLC E D252 S377 D250 S375
BS04 GLC E D252 G345 F368 D250 G343 F366
BS05 AC1 E D251 D252 W260 H296 E342 L344 D249 D250 W258 H294 E340 L342
Gene Ontology
Molecular Function
GO:0004134 4-alpha-glucanotransferase activity
GO:0016757 glycosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6m6t, PDBe:6m6t, PDBj:6m6t
PDBsum6m6t
PubMed33762620
UniProtA0A0E1EIJ0

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