Structure of PDB 2amg Chain A Binding Site BS02

Receptor Information
>2amg Chain A (length=415) Species: 316 (Stutzerimonas stutzeri) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADG
FSAIWMPVPWRDFSSWSKSGGGEGYFWHDFNKNGRYGSDAQLRQAASALG
GAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDG
DRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAPERV
NSWMTDSADNSFCVGELWKGPSEYPNWDWRNTASWQQIIKDWSDRAKCPV
FDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPGQNG
GQHHWALQDGLIRQAYAYILTSPGTPVVYWDHMYDWGYGDFIRQLIQVRR
AAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASGSFS
EAVNASNGQVRVWRS
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2amg Chain A Residue 452 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2amg Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D1 Q2 H13 D16 E17
Binding residue
(residue number reindexed from 1)		D1 Q2 H13 D16 E17
Annotation score4
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.
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0043169 cation binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
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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