Structure of PDB 2amg Chain A

Receptor sequence
>2amgA (length=415) Species: 316 (Stutzerimonas stutzeri) [Search protein sequence]
DQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADG
FSAIWMPVPWRDFSSWSKSGGGEGYFWHDFNKNGRYGSDAQLRQAASALG
GAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDG
DRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAPERV
NSWMTDSADNSFCVGELWKGPSEYPNWDWRNTASWQQIIKDWSDRAKCPV
FDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPGQNG
GQHHWALQDGLIRQAYAYILTSPGTPVVYWDHMYDWGYGDFIRQLIQVRR
AAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASGSFS
EAVNASNGQVRVWRS
3D structure
PDB2amg Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
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) D193 E219 D294
Catalytic site (residue number reindexed from 1) D190 E216 D291
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 CA A N116 D151 D154 D162 G197 N113 D148 D151 D159 G194
BS02 CA A D1 Q2 H13 D16 E17 D1 Q2 H13 D16 E17
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0043169 cation binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2amg, PDBe:2amg, PDBj:2amg
PDBsum2amg
PubMed9126844
UniProtP13507|AMT4_STUST Glucan 1,4-alpha-maltotetraohydrolase (Gene Name=amyP)

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