Structure of PDB 4maz Chain A Binding Site BS01

Receptor Information
>4maz Chain A (length=559) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EWWKEAVVYQIYPRSFYDANGDGFGDLQGVIQKLDYIKNLGADVIWLSPV
FDSPQDDNGYDISDYKNMYEKFGTNEDMFQLIDEVHKRGMKIVMDLVVNH
TSDEHAWFAESRKSKDNPYRDYYLWKDPKPDGSEPNNWGSIFSGSAWTYD
EGTGQYYLHYFSKKQPDLNWENEAVRREVYDVMRFWMDRGVDGWRMDSIG
SISKYTDFPDYETDHSRSYIVGRYHSNGPRLHEFIQEMNREVLSHYDCMT
VGEANGSDIEEAKKYTDASRQELNMIFTFEHMDIDKEQNSPNGKWQIKPF
DLIALKKTMTRWQTGLMNVGWNTLYFENHDQPRVISRWGNDRKLRKECAK
AFATVLHGMKGTPFIYQGEEIGMVNSDMPLEMYDDLEIKNAYRELVVENK
TMSEKEFVKAVMIKGRDHARTPMQWDAGKHAGFTAGDPWIPVNSRYQDIN
VKESLEDQDSIFFYYQKLIQLRKQYKIMIYGDYQLLQENDPQVFSYLREY
RGEKLLVVVNLSEEKALFEAPPELIHERWKVLISNYPQERADLKSISLKP
YEAVMGISI
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain4maz Chain A Residue 604 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4maz Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed rates.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		D20 N22 D24 F26 D28
Binding residue
(residue number reindexed from 1)		D18 N20 D22 F24 D26
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D97 R197 D199 E255 H331 D332
Catalytic site (residue number reindexed from 1) D95 R195 D197 E253 H329 D330
Enzyme Commision number 3.2.1.10: oligo-1,6-glucosidase.
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0004574 oligo-1,6-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4maz, PDBe:4maz, PDBj:4maz
PDBsum4maz
PubMed24015933
UniProtO06994|O16G1_BACSU Oligo-1,6-glucosidase 1 (Gene Name=malL)

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