Structure of PDB 6a0k Chain B Binding Site BS06

Receptor Information

>6a0k Chain B (length=442) Species: 1665 (Arthrobacter globiformis)

TAPDWLADAVFYQIFPERFANADPSLDPQNVVPWGSTPTPDNFFGGDLQG
IIDHLDHIVALGANALYLTPIFEADTNHRYDAKDYFSIDHRLGTLETFHA
LMAECRARGIRIVLDAVLNHCGDGHWAFADVVENEADSAYVNWFSVEGFP
VTAHPTPNYRTCSGCYYLPKWNAYNPEVRHHHLDVARYWIDQGIDGWRLD
VPYFINHTFWREFRTAVKGKSEDLYIVAEEWRSPVEWLQGDTADGTMNYT
ARDLILGFTADGGIDASALAAGLNALHAEIPAGFHRGMLNLLGSHDTERV
LTRHAGDVEAALLSYALLFSLEGAPMVYYGDEVGLTGDNDPGCRGAMPWN
EESWNTRLLDGIRTFAAFRAHQPAMRRGRQTAVALDADTIAIVRSGGDER
AAVIVHRGEGTTVDTASIPELAPLDADTVVLGPLGTASLATA

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 6a0k Chain B Residue 507

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6a0k Structural features of a bacterial cyclic alpha-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis.
• Resolution: 1.94 Å
• Binding residue (original residue number in PDB): N22 D24 D28 G46 D48
• Binding residue (residue number reindexed from 1): N21 D23 D27 G45 D47
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): D116 R199 D201 E230 H296 D297
• Catalytic site (residue number reindexed from 1): D115 R198 D200 E229 H295 D296

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:6a0k, PDBe:6a0k, PDBj:6a0k
• PDBsum: 6a0k
• PubMed: 30181215
• UniProt: D2YYE1