Structure of PDB 1qpk Chain A

Receptor sequence
>1qpkA (length=418) Species: 316 (Stutzerimonas stutzeri) [Search protein sequence]
DQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADG
FSAIWMPVPWRDFSSWSDGSKSGGGEGYFWHDFNKNGRYGSDAQLRQAAS
ALGGAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDC
DDGDRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFGFVRGYAP
ERVNSWMTDSADNSFCVGELWKGPSEYPNWDWRNTASWQQIIKDWSDRAK
CPVFDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPG
QNGGQHHWALQDGLIRQAYAYILTSPGTPVVYWDHMYDWGYGDFIRQLIQ
VRRAAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASG
SFSEAVNASNGQVRVWRS
3D structure
PDB1qpk Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G193 E219 D294
Catalytic site (residue number reindexed from 1) G193 E219 D294
Enzyme Commision number 3.2.1.60: glucan 1,4-alpha-maltotetraohydrolase.
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 Y78 H117 R191 E219 H293 D294 Y78 H117 R191 E219 H293 D294
BS02 GLC A W25 Y78 Q305 W25 Y78 Q305
BS03 GLC A W66 F79 I157 W66 F79 I157
BS04 GLC A F79 I157 G158 D160 A161 F79 I157 G158 D160 A161
BS05 CA A N116 D151 D154 D162 G197 N116 D151 D154 D162 G197
BS06 CA A D1 Q2 H13 G14 D16 E17 D1 Q2 H13 G14 D16 E17
Gene Ontology
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Biological Process
External links
PDB RCSB:1qpk, PDBe:1qpk, PDBj:1qpk
PDBsum1qpk
PubMed10556241
UniProtP13507|AMT4_STUST Glucan 1,4-alpha-maltotetraohydrolase (Gene Name=amyP)

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