Structure of PDB 4m8u Chain A Binding Site BS01

Receptor Information
>4m8u 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]
SEWWKEAVVYQIYPRSFYDANGDGFGDLQGVIQKLDYIKNLGADVIWLSP
VFDSPQDDNGYDISDYKNMYEKFGTNEDMFQLIDEVHKRGMKIVMDLVVN
HTSDEHAWFAESRKSKDNPYRDYYLWKDPKPDGSEPNNWGSIFSGSAWTY
DEGTGQYYLHYFSKKQPDLNWENEAVRREVYDVMRFWMDRGVDGWRMDAI
GSISKYTDFPDYETDHSRSYIVGRYHSNGPRLHEFIQEMNREVLSHYDCM
TVGEANGSDIEEAKKYTDASRQELNMIFTFEHMDIDKEQNSPNGKWQIKP
FDLIALKKTMTRWQTGLMNVGWNTLYFENHDQPRVISRWGNDRKLRKECA
KAFATVLHGMKGTPFIYQGEEIGMVNSDMPLEMYDDLEIKNAYRELVVEN
KTMSEKEFVKAVMIKGRDHARTPMQWDAGKHAGFTAGDPWIPVNSRYQDI
NVKESLEDQDSIFFYYQKLIQLRKQYKIMIYGDYQLLQENDPQVFSYLRE
YRGEKLLVVVNLSEEKALFEAPPELIHERWKVLISNYPERADLKSISLKP
YEAVMGISI
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 chain4m8u Chain A Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4m8u Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed rates.
Resolution1.45 Å
Binding residue
(original residue number in PDB)		D20 N22 D24 F26 D28
Binding residue
(residue number reindexed from 1)		D19 N21 D23 F25 D27
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D97 R197 D199 E255 H331 D332
Catalytic site (residue number reindexed from 1) D96 R196 D198 E254 H330 D331
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4m8u, PDBe:4m8u, PDBj:4m8u
PDBsum4m8u
PubMed24015933
UniProtO06994|O16G1_BACSU Oligo-1,6-glucosidase 1 (Gene Name=malL)

[Back to BioLiP]