Structure of PDB 1esw Chain A

Receptor sequence

>1eswA (length=500) Species: 271 (Thermus aquaticus)

MELPRAFGLLLHPTSLPGPYGVGVLGREARDFLRFLKEAGGRYWQVLPLG
PTGYGDSPYQSFSAFAGNPYLIDLRPLAERGYVRLEDPGFPQGRVDYGLL
YAWKWPALKEAFRGFKEKASPEEREAFAAFREREAWWLEDYALFMALKGA
HGGLPWNRWPLPLRKREEKALREAKSALAEEVAFHAFTQWLFFRQWGALK
AEAEALGIRIIGDMPIFVAEDSAEVWAHPEWFHLDEEGRPTVVAGVPPDY
FSETGQRWGNPLYRWDVLEREGFSFWIRRLEKALELFHLVRIDHFRGFEA
YWEIPASCPTAVEGRWVKAPGEKLFQKIQEVFGEVPVLAEDLGVITPEVE
ALRDRFGLPGMKVLQFAFDDGMENPFLPHNYPAHGRVVVYTGTHDNDTTL
GWYRTATPHEKAFMARYLADWGITFREEEEVPWALMHLGMKSVARLAVYP
VQDVLALGSEARMNYPGRPSGNWAWRLLPGELSPEHGARLRAMAEATERL

3D structure

• PDB: 1esw X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D293 E340 D395
• Catalytic site (residue number reindexed from 1): D293 E340 D395
• 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	GLC	A	Q256 W258 H294 E340	Q256 W258 H294 E340
BS02	GLC	A	Y59 W258 H394 D395	Y59 W258 H394 D395
BS03	AC1	A	S57 Q60 N464	S57 Q60 N464
BS04	GLC	A	G53 Y54 Y101	G53 Y54 Y101
BS05	AC1	A	Y54 G55 D56 G98 S470	Y54 G55 D56 G98 S470

Gene Ontology

Molecular Function

• GO:0004134 4-alpha-glucanotransferase activity
• GO:0016757 glycosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1esw, PDBe:1esw, PDBj:1esw
• PDBsum: 1esw
• PubMed: 11082203
• UniProt: O87172|MALQ_THETH 4-alpha-glucanotransferase (Gene Name=malQ)