Structure of PDB 3u95 Chain D Binding Site BS01

Receptor Information

>3u95 Chain D (length=468) Species: 309803 (Thermotoga neapolitana DSM 4359)

MKISIVGAGSVRFALQLVEDIAQTDELSREDTHIYLMDVHERRLNASYIL
ARKYVEELNSPVKVVKTESLDEAIEGADFIINTAYPYDPRYHDSGSQRWD
EVTKVGEKHGYYRGIDSQELNMVSTYTYVLSSYPDVKLALEIAEKMKKMA
PKAYLMQTANPVFEITQAVRRWTGANIIGFCHGVAGVYEVFERLGLDPEE
VDWQVAGVNHGIWLNRFRYRGKDAYPLLDEWIEKELSKWEPKNPWDTQMS
PAAMDMYRFYGMLPIGDTVRNGTWKYHYNLETKKKWFRRFGGIDNEVERP
KFHEHLRRARERLIKLAEEVQENPHLKITEKHPEIFPKGRLSGEQHIPFI
NAIANNKRVRLFLNVENQGALKDFPDDLVMELPVWVDSSGIHREKVEPDL
THRIKIFYLWPRILRTEWNLEAFISRDRKVLEEILIRDPRTKSYEQVVKV
LDEILSLPFNEEIRRYYE

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 3u95 Chain D Residue 600

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3u95 Crystal structure and thermostability of a putative alpha-glucosidase from Thermotoga neapolitana
• Resolution: 1.998 Å
• Binding residue (original residue number in PDB): C181 H210
• Binding residue (residue number reindexed from 1): C181 H210
• Annotation score: 4

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:3u95, PDBe:3u95, PDBj:3u95
• PDBsum: 3u95
• PubMed: 22093829
• UniProt: B9KAM3