Structure of PDB 5jiw Chain A

Receptor sequence
>5jiwA (length=500) Species: 271 (Thermus aquaticus) [Search protein sequence]
MELPRAFGLLLHPTSLPGPYGVGVLGREARDFLRFLKEAGGRYWQVLPLG
PTGYGDSPYQSFSAFAGNPYLIDLRPLAERGYVRLEDPGFPQGRVDYGLL
YAWKWPALKEAFRGFKEKASPEEREAFAAFREREAWWLEDYALFMALKGA
HGGLPWNRWPLPLRKREEKALREAKSALAEEVAFHAFTQWLFFRQWGALK
AEAEALGIRIIGDMPIFVAEDSAEVWAHPEWFHLDEEGRPTVVAGVPPDY
FSETGQRWGNPLYRWDVLEREGFSFWIRRLEKALELFHLVRIAHFRGFEA
YWEIPASCPTAVEGRWVKAPGEKLFQKIQEVFGEVPVLAEDLGVITPEVE
ALRDRFGLPGMKVLQFAFDcGMENPFLPHNYPAHGRVVVYTGTHNNDTTL
GWYRTATPHEKAFMARYLADWGITFREEEEVPWALMHLGMKSVARLAVYP
VQDVLALGSEARMNYPGRPSGNWAWRLLPGELSPEHGARLRAMAEATERL
3D structure
PDB5jiw Amylose recognition and ring-size determination of amylomaltase.
ChainA
Resolution1.73 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A293 E340 N395
Catalytic site (residue number reindexed from 1) A293 E340 N394
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 X370 N374 X370 N374
BS02 GLC A G343 D369 F376 G343 D369 F376
BS03 GLC A F251 G343 F251 G343
BS04 GLC A Q256 W258 H294 E340 Q256 W258 H294 E340
BS05 GLC A H394 N395 H394 N395
BS06 GLC A S57 Y59 Q60 N464 S57 Y59 Q60 N464
BS07 GLC A F62 G153 F62 G153
BS08 GLC A G55 D56 G55 D56
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5jiw, PDBe:5jiw, PDBj:5jiw
PDBsum5jiw
PubMed28097217
UniProtO87172|MALQ_THETH 4-alpha-glucanotransferase (Gene Name=malQ)

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