Structure of PDB 1mxd Chain A Binding Site BS12

Receptor Information

>1mxd Chain A (length=435) Species: 2262 (Pyrococcus woesei)

AKYLELEEGGVIMQAFYWDVPGGGIWWDHIRSKIPEWYEAGISAIWLPPP
SKGMSGGYSMGYDPYDYFDLGEYYQKGTVETRFGSKEELVRLIQTAHAYG
IKVIADVVINHRAGGDLEWNPFVGDYTWTDFSKVASGKYTANYLDFHPNE
LHCCDEGTFGGFPDICHHKEWDQYWLWKSNESYAAYLRSIGFDGWRFDYV
KGYGAWVVRDWLNWWGGWAVGEYWDTNVDALLSWAYESGAKVFDFPLYYK
MDEAFDNNNIPALVYALQNGQTVVSRDPFKAVTFVANHDTDIIWNKYPAY
AFILTYEGQPVIFYRDFEEWLNKDKLINLIWIHDHLAGGSTTIVYYDNDE
LIFVRNGDSRRPGLITYINLSPNWVGRWVYVPKFAGACIHEYTGNLGGWV
DKRVDSSGWVYLEAPPHDPANGYYGYSVWSYCGVG

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 1mxd Chain A Residue 727

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1mxd Differential Regulation of a Hyperthermophilic alpha-Amylase with a Novel (Ca,Zn) Two-metal Center by Zinc
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): E36 E318 K323
• Binding residue (residue number reindexed from 1): E36 E318 K323
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): D198 E222 D289
• Catalytic site (residue number reindexed from 1): D198 E222 D289
• Enzyme Commision number: 3.2.1.1: alpha-amylase.

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0004556 alpha-amylase activity
• GO:0005509 calcium ion binding
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0043169 cation binding
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:1mxd, PDBe:1mxd, PDBj:1mxd
• PDBsum: 1mxd
• PubMed: 12482867
• UniProt: Q7LYT7