Structure of PDB 6gya Chain C

Receptor sequence
>6gyaC (length=481) Species: 61169 (Alicyclobacillus sp.) [Search protein sequence]
GDNGTMMQYFEWYLPNDGTLWTKMGSDASHLKSIGITGVWFPPAYKGQSQ
SDVGYGVYDMYDLGEFNQKGTVRTKYGTKAQLQSAITSLHNNGIQAYGDV
VLNHRMGADATETISAVEVNPSNRNQVTSGAYNISAWTDFEFPGRGNTYS
SFKWHSYYFDGVDWDQSRQLSGKIYQIQGKAWDWEVDSENGNYDYLMGAD
IDYDHPDVQTEVKNWGKWFVNTLNLDGVRLDAVKHIKFDYMSSWLSSVKS
TTGKSNLFAVGEYWNTSLGALENYENKTNWSMSLFDVPLHMNFQAAANGG
GYYDMRNLLNNTMMKNHPIQAVTFVDNHDTEPGQALQSWVSDWFKPLAYA
TILTRQEGYPCVFYGDYYGIPSQSVSAKSTWLDKQLSARKSYAYGTQHDY
LDNQDVIGWTREGDSAHAGSGLATVMSDGPGGSKTMYVGTAHAGQVFKDI
TGNRTDTVTINSAGNGTFPCNGGSVSIWVKQ
3D structure
PDB6gya The structure of the AliC GH13 alpha-amylase from Alicyclobacillus sp. reveals the accommodation of starch branching points in the alpha-amylase family.
ChainC
Resolution2.95 Å
3D
structure
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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 C L199 H238 E265 L196 H235 E262
BS02 CA C N106 D197 D203 H238 N103 D194 D200 H235
BS03 CA C D163 A184 D186 D205 D207 D160 A181 D183 D202 D204
BS04 CA C G304 Y305 Y306 Q407 D408 D431 G301 Y302 Y303 Q404 D405 D428
BS05 GLC C Q98 F261 Q95 F258
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0005509 calcium ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:6gya, PDBe:6gya, PDBj:6gya
PDBsum6gya
PubMed30644839
UniProtA0A3P8MUS3

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