Structure of PDB 4m8u Chain A

Receptor sequence

>4m8uA (length=559) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168)

SEWWKEAVVYQIYPRSFYDANGDGFGDLQGVIQKLDYIKNLGADVIWLSP
VFDSPQDDNGYDISDYKNMYEKFGTNEDMFQLIDEVHKRGMKIVMDLVVN
HTSDEHAWFAESRKSKDNPYRDYYLWKDPKPDGSEPNNWGSIFSGSAWTY
DEGTGQYYLHYFSKKQPDLNWENEAVRREVYDVMRFWMDRGVDGWRMDAI
GSISKYTDFPDYETDHSRSYIVGRYHSNGPRLHEFIQEMNREVLSHYDCM
TVGEANGSDIEEAKKYTDASRQELNMIFTFEHMDIDKEQNSPNGKWQIKP
FDLIALKKTMTRWQTGLMNVGWNTLYFENHDQPRVISRWGNDRKLRKECA
KAFATVLHGMKGTPFIYQGEEIGMVNSDMPLEMYDDLEIKNAYRELVVEN
KTMSEKEFVKAVMIKGRDHARTPMQWDAGKHAGFTAGDPWIPVNSRYQDI
NVKESLEDQDSIFFYYQKLIQLRKQYKIMIYGDYQLLQENDPQVFSYLRE
YRGEKLLVVVNLSEEKALFEAPPELIHERWKVLISNYPERADLKSISLKP
YEAVMGISI

3D structure

• PDB: 4m8u Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed rates.
• Chain: A
• Resolution: 1.45 Å

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.

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	D20 N22 D24 F26 D28	D19 N21 D23 F25 D27

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

External links

• PDB: RCSB:4m8u, PDBe:4m8u, PDBj:4m8u
• PDBsum: 4m8u
• PubMed: 24015933
• UniProt: O06994|O16G1_BACSU Oligo-1,6-glucosidase 1 (Gene Name=malL)