Structure of PDB 5awq Chain A

Receptor sequence
>5awqA (length=596) Species: 1665 (Arthrobacter globiformis) [Search protein sequence]
PVTAAPPLRLASRNSVFTRSGAGPRYWNIYGYSFPHNAPIPENEWKVNID
WLAGNFADFGYDIACTDGWIEGSSRTTGNGYITSYNDSWQHDWAYWANYL
AARKMKLGVYYNPLWVHRAAVEDASKTVLGRPDVKIADLVVPGDFFARDI
GGNQLYWLDVTKSGAKEYVQGYVRYFKDLGVPYLRIDFLSWYEDGRDANI
GQVNAPHGRANYELALSWINEAAGEDMEVSLVMPHMFQDGSAELANGDLV
RINADADKGGWDRLSGMRQNWQDAWPNWANPFCGFTGWSHRNGRGQLILD
GDFMRASTFASDEERKTMMNLMVAAGSPLAIADTYQQIGNNAWVYTNKEV
LQLNADGLVGKPLYRSATPFSKDPGSRDTERWAGQLPDGSWGVALFNRSD
TETVTKTIDFAKDLGLATGGNVRDLWEHRNLGMDSRATAALAPHASAIFR
VTPPKMHGTTRYPAAFAAWGGGAGFNYNHPGYDGNGFVDGLQAGSGSADP
LVTFAVQVPHRGSYAIRYRYANATGDTSTMTVTAEKADRSTVDGPVHVSF
PGLATWDTWGVADGTITLDAGLNLVTIGRGATDKGAINLNWIELDM
3D structure
PDB5awq Crystal Structure and Mutational Analysis of Isomalto-dextranase, a Member of Glycoside Hydrolase Family 27
ChainA
Resolution1.48 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number ?
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 D207 D265 D197 D255
BS02 GLC A Y40 D77 D197 F198 D265 Y30 D67 D187 F188 D255
BS03 GLC A G78 W79 I80 E81 G68 W69 I70 E71
BS04 GLC A H489 Q502 W566 A596 N598 H479 Q492 W556 A586 N588
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5awq, PDBe:5awq, PDBj:5awq
PDBsum5awq
PubMed26330557
UniProtQ7WSN5

[Back to BioLiP]