Structure of PDB 1jdd Chain A Binding Site BS05

Receptor Information
>1jdd Chain A (length=418) Species: 316 (Stutzerimonas stutzeri) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADG
FSAIWMPVPWRDFSSWSDGSKSGGGEGYFWHDFNKNGRYGSDAQLRQAAS
ALGGAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDC
DDGDRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAP
ERVNSWMTDSADNSFCVGQLWKGPSEYPNWDWRNTASWQQIIKDWSDRAK
CPVFDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPG
QNGGQHHWALQDGLIRQAYAYILTSPGTPVVYWDHMYDWGYGDFIRQLIQ
VRRAAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASG
SFSEAVNASNGQVRVWRS
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 chain1jdd Chain A Residue 451 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1jdd Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		N116 D151 D154 D162 G197
Binding residue
(residue number reindexed from 1)		N116 D151 D154 D162 G197
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D193 Q219 D294
Catalytic site (residue number reindexed from 1) D193 Q219 D294
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1jdd, PDBe:1jdd, PDBj:1jdd
PDBsum1jdd
PubMed9281429
UniProtP13507|AMT4_STUST Glucan 1,4-alpha-maltotetraohydrolase (Gene Name=amyP)

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