Alpha-amylase B in complex with acarbose

6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucose; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-D-glucose; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-glucose

alpha-D-quinovose; 6-deoxy-alpha-D-glucopyranose; D-quinovose; quinovose; 6-DEOXY-ALPHA-D-GLUCOSE

4,6-DIDEOXYGLUCOSE; 4,6-dideoxy-alpha-D-xylo-hexose; 4,6-dideoxy-D-xylo-hexose; 4,6-dideoxy-xylo-hexose

Crystal Structure of the Polyextremophilic alpha-Amylase AmyB from Halothermothrix orenii: Details of a Productive Enzyme-Substrate Complex and an N Domain with a Role in Binding Raw Starch

GLC A 1002 HAS WRONG CHIRALITY AT ATOM C1

Si(111) double crystal monochromator, water-cooled

GCSNISEDVNNPNRSLFLIESEPSTGASVSKNLTEIILIFSNDINKVSQLALTDLITDSDIQGIDYNIEGNKVIINNFSL
EPTCNYRLSYEVIDIYDNHLQGYIEFLVNQSNYPQIPDQEVNHTILQAFYWEMNTGEYATEHPEEANLWNLLAERAPELA
EAGFTAVWLPPANKGMAGIHDVGYGTYDLWDLGEFDQKGTVRTKYGTKGELENAIDALHNNDIKVYFDAVLNHRMGADYA
ETVLLDENSRDKPGQYIKAWTGFNFPGRNGEYSNFTWNGQCFDGTDWDDYSKESGKYLFDEKSWDWTYNWDEDYLMGADV
DYENEAVQNDVIDWGQWIINNIDFDGFRLDAVKHIDYRFIDKWMSAVQNSSNRDVFFVGEAWVEDVDDLKGFLDTVGNPD
LRVFDFPLRSFFVDMLNGAYMADLRNAGLVNSPGYENRAVTFVDNHDTDRDEGSYTVSIYSRKYQAYAYILTRAEGVPTV
YWKDYYIWEMKEGLDKLLTARRYYAYGPGYEVDNNDADIYSYVRSGFPDVAGDGLVLMISDGTSGNVAGKWINSRQPDTE
FYDLTGHIKEHVTTDSEGYGNFKVIKSEDKGWSIWVPVE

0.2M sodium acetate, 0.1M Mes-OH, 20% (w/v) PEG 8000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Alpha-amylase B in complex with maltotetraose and alpha-cyclodextrin

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

alpha-amylase, acarbose, thermostable, halophilic, N domain, raw starch binding, HYDROLASE