Structure of PDB 7lv6 Chain B

Receptor sequence
>7lv6B (length=559) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
EWWKEAVVYQIYPRSFYDANGDGFGDLQGVIQKLDYIKNLGADVIWLSPV
FDSPQDDNGYDISDYKNMYEKFGTNEDMFQLIDEVHKRGMKIVMDLVVNH
TSDEHAWFAESRKSKDNPYRDYYLWKDPKPDGSEPNNWGSIFSGSAWTYD
EGTGQYYLHYFSKKQPDLNWENEAVRREVYDVMRFWMDRGVDGWRMDVIG
SISKYTDFPDYETDHSRSYIVGRYHSNGPRLHEFIQEMNREVLSHYDCMT
VGEANGSDIEEAKKYTDASRQELNMIFTFEHMDIDKEQNSPNGKWQIKPF
DLIALKKTMTRWQTGLMNVGWNTLYFENHDQPRVISRWGNDRKLRKECAK
AFATVLHGMKGTPFIYQGEEIGMVNSDMPLEMYDDLEIKNAYRELVVENK
TMSEKEFVKAVMIKGRDHARTPMQWDAGKHAGFTAGDPWIPVNSRYQDIN
VKESLEDQDSIFFYYQKLIQLRKQYKIMIYGDYQLLQENDPQVFSYLREY
RGEKLLVVVNLSEEKALFEAPPELIHERWKVLIRNYPQERADLKSISLKP
YEAVMGISI
3D structure
PDB7lv6 Urea binding to guide rational design of mutations that influence enzyme dynamics
ChainB
Resolution1.1 Å
3D
structure
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Enzymatic activity
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 B D20 N22 D24 F26 D28 D18 N20 D22 F24 D26
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:7lv6, PDBe:7lv6, PDBj:7lv6
PDBsum7lv6
PubMed
UniProtO06994|O16G1_BACSU Oligo-1,6-glucosidase 1 (Gene Name=malL)

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