Structure of PDB 5mac Chain A Binding Site BS02

Receptor Information

>5mac Chain A (length=473) Species: 29291 (Methanococcoides burtonii)

MSLIYEDLVKSLDSKQQAYVDLKLPDPTNGEFLLAVFHMIPGGDLNVLQA
AAEIAAESSTGTNIKVSTETAFSRTMNARVYQLDLERELVWIAYPWRLFD
RGGNVQNILTYIIGNILGMKEIQALKLMDIWFPPSMLEQYDGPSYTVDDM
RKYLDVYDRPILGTIVKPKMGLTSAEYAEVCYDFWVGGGDFVKNDEPQAN
QDFCPYEKMVAHVKEAMDKAVKETGQKKVHSFNVSAADFDTMIERCEMIT
NAGFEPGSYAFLIDGITAGWMAVQTLRRRYPDVFLHFHRAAHGAFTRQEN
PIGFSVLVLSKFARLAGASGIHTGTAGIGKMKGTPAEDVVAAHSIQYLKS
PGHFFEQTWSKIMDTDKDVINLVNEDLAHHVILEDDSWRAMKKCCPIVSG
GLNPVKLKPFIDVMENVDFITTMGSGVHSHPGGTQSGAKALVQACDAYLQ
GMDIEEYAKDHKELAEAIEFYLN

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 5mac Chain A Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5mac A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic.
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): K193 D195 E196
• Binding residue (residue number reindexed from 1): K193 D195 E196
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): K167 K193 N194 D195 E196 H288 H322 K330
• Catalytic site (residue number reindexed from 1): K167 K193 N194 D195 E196 H288 H322 K330
• Enzyme Commision number: 4.1.1.39: ribulose-bisphosphate carboxylase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0016829 lyase activity
• GO:0016984 ribulose-bisphosphate carboxylase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0015977 carbon fixation

External links

• PDB: RCSB:5mac, PDBe:5mac, PDBj:5mac
• PDBsum: 5mac
• PubMed: 28154188
• UniProt: Q12TQ0