Structure of PDB 2aaa Chain A

Receptor sequence

>2aaaA (length=476) Species: 5061 (Aspergillus niger)

LSAASWRTQSIYFLLTDRFGRTDNSTTATCNTGNEIYCGGSWQGIIDHLD
YIEGMGFTAIWISPITEQLPQDTADGEAYHGYWQQKIYDVNSNFGTADNL
KSLSDALHARGMYLMVDVVPDHMGYAGNGNDVDYSVFDPFDSSSYFHPYC
LITDWDNLTMVEDCWEGDTIVSLPDLDTTETAVRTIWYDWVADLVSNYSV
DGLRIDSVLEVQPDFFPGYNKASGVYCVGEIDNGNPASDCPYQKVLDGVL
NYPIYWQLLYAFESSSGSISNLYNMIKSVASDCSDPTLLGNFIENHDNPR
FAKYTSDYSQAKNVLSYIFLSDGIPIVYAGEEQHYAGGKVPYNREATWLS
GYDTSAELYTWIATTNAIRKLAIAADSAYITYANDAFYTDSNTIAMAKGT
SGSQVITVLSNKGSSGSSYTLTLSGSGYTSGTKLIEAYTCTSVTVDSSGD
IPVPMASGLPRVLLPASVVDSSSLCG

3D structure

• PDB: 2aaa Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus.
• Chain: A
• Resolution: 2.12 Å

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.

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	D121 E162 D175 E210	D121 E162 D175 E210
BS02	CA	A	D206 E230	D206 E230

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

External links

• PDB: RCSB:2aaa, PDBe:2aaa, PDBj:2aaa
• PDBsum: 2aaa
• PubMed: 2207069
• UniProt: P56271|AMYA_ASPNG Acid alpha-amylase