Structure of PDB 2aaa Chain A Binding Site BS01

Receptor Information
>2aaa Chain A (length=476) Species: 5061 (Aspergillus niger) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LSAASWRTQSIYFLLTDRFGRTDNSTTATCNTGNEIYCGGSWQGIIDHLD
YIEGMGFTAIWISPITEQLPQDTADGEAYHGYWQQKIYDVNSNFGTADNL
KSLSDALHARGMYLMVDVVPDHMGYAGNGNDVDYSVFDPFDSSSYFHPYC
LITDWDNLTMVEDCWEGDTIVSLPDLDTTETAVRTIWYDWVADLVSNYSV
DGLRIDSVLEVQPDFFPGYNKASGVYCVGEIDNGNPASDCPYQKVLDGVL
NYPIYWQLLYAFESSSGSISNLYNMIKSVASDCSDPTLLGNFIENHDNPR
FAKYTSDYSQAKNVLSYIFLSDGIPIVYAGEEQHYAGGKVPYNREATWLS
GYDTSAELYTWIATTNAIRKLAIAADSAYITYANDAFYTDSNTIAMAKGT
SGSQVITVLSNKGSSGSSYTLTLSGSGYTSGTKLIEAYTCTSVTVDSSGD
IPVPMASGLPRVLLPASVVDSSSLCG
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 chain2aaa Chain A Residue 485 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2aaa Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus.
Resolution2.12 Å
Binding residue
(original residue number in PDB)		D121 E162 D175 E210
Binding residue
(residue number reindexed from 1)		D121 E162 D175 E210
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) R204 D206 E230 H296 D297
Catalytic site (residue number reindexed from 1) R204 D206 E230 H296 D297
Enzyme Commision number 3.2.1.1: alpha-amylase.
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2aaa, PDBe:2aaa, PDBj:2aaa
PDBsum2aaa
PubMed2207069
UniProtP56271|AMYA_ASPNG Acid alpha-amylase

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