Structure of PDB 6tp0 Chain A

Receptor sequence
>6tp0A (length=481) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
LNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQD
DVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAINSLHSRDINVYGDVV
INHKGGADATEYVTAVEVDPADRNRVTSGEQRIKAWTHFQFPGRGSTYSD
FKWYWYHFDGTDWDESRKLNRIYKFQGKAWDWEVSNENGNYDYLMYADID
YDHPDVTAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKT
GKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGY
DMRKLLNGTVVSKHPVKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFIL
TREAGYPQIFYGDMYGTKGASQREIPALKHKIEPILKARKQYAYGAQHDY
FDHHNIVGWTREGDSSVANSGLAALITDGPGGTKRMYVGRQNAGETWHDI
TGNRSDSVVINAEGWGEFHVNGGSVSIYVQR
3D structure
PDB6tp0 Characterization of the starch surface binding site on Bacillus paralicheniformis alpha-amylase.
ChainA
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R229 D231 E261 H327 D328
Catalytic site (residue number reindexed from 1) R227 D229 E259 H325 D326
Enzyme Commision number 3.2.1.1: alpha-amylase.
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 G5 F257 V318 Y358 G3 F255 V316 Y356
BS02 GLC A T38 E255 Y358 T36 E253 Y356
BS03 CA A N104 D194 D200 H235 N102 D192 D198 H233
BS04 CA A D161 A181 D183 D202 D204 D159 A179 D181 D200 D202
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal 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:6tp0, PDBe:6tp0, PDBj:6tp0
PDBsum6tp0
PubMed33058974
UniProtI3P686

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