Structure of PDB 5zxg Chain A Binding Site BS01

Receptor Information

>5zxg Chain A (length=440) Species: 1665 (Arthrobacter globiformis)

PDWLADAVFYQIFPERFANADPSLDPQNVVPWGSTPTPDNFFGGDLQGII
DHLDHIVALGANALYLTPIFEADTNHRYDAKDYFSIDHRLGTLETFHALM
AECRARGIRIVLDAVLNHCGDGHWAFADVVENEADSAYVNWFSVEGFPVT
AHPTPNYRTCSGCYYLPKWNAYNPEVRHHHLDVARYWIDQGIDGWRLDVP
YFINHTFWREFRTAVKGKSEDLYIVAEEWRSPVEWLQGDTADGTMNYTAR
DLILGFTADGGIDASALAAGLNALHAEIPAGFHRGMLNLLGSHDTERVLT
RHAGDVEAALLSYALLFSLEGAPMVYYGDEVGLTGDNDPGCRGAMPWNEE
SWNTRLLDGIRTFAAFRAHQPAMRRGRQTAVALDADTIAIVRSGGDERAA
VIVHRGEGTTVDTASIPELAPLDADTVVLGPLGTASLATA

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: 5zxg Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5zxg Structural features of a bacterial cyclic alpha-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis.
• Resolution: 2.4 Å
• Binding residue (original residue number in PDB): N23 D25 D29 G47 D49
• Binding residue (residue number reindexed from 1): N19 D21 D25 G43 D45
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): D117 R200 D202 E231 H297 D298
• Catalytic site (residue number reindexed from 1): D113 R196 D198 E227 H293 D294

Gene Ontology

Molecular Function

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

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:5zxg, PDBe:5zxg, PDBj:5zxg
• PDBsum: 5zxg
• PubMed: 30181215
• UniProt: D2YYE1