Structure of PDB 5c2g Chain E Binding Site BS03

Receptor Information

>5c2g Chain E (length=457) Species: 96 (Gallionella)

GSHMDQSNRYADLSLKEEDLIKGGNHILVAYTMEPAAGVGYLEAAAHIAA
ESSTGTNVEVSTTDEFTKGVDALVYFIDEAKGIMKVAYPNDLFDRNVTDG
RVMIVSFLTLCIGNNQGMGDIANLQMQDFYVPPRMLQLFDGPAKDISDLW
RILGRPVKDGGYISGTIIKPKLGLRPEPFAKAAYQFWLGGDFIKNDEPQG
NQVFCPIKKVLPLVYDSLKRAQDETGQAKLFSMNITADDHYEMCARADFA
LETFGPDADKVAFLVDGFVGGPGMVTTARRQYPSQYLHYHRAGHGMVTSP
SSKRGYTAFVLAKMSRLQGASGIHVGTMGYGKMEGGKDDRIIAYMIERDS
CTGPFYHQEWYGMKPTTPIISGGMNALRLPGFFENLGHGNVINTAGGGSY
GHIDSPAAGAVSLRQAYECWKAGADPIEWAKEHKEFARAFESFPKDADKL
FPGWREK

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: 5c2g Chain E Residue 801

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5c2g Functional metagenomic selection of ribulose 1, 5-bisphosphate carboxylase/oxygenase from uncultivated bacteria.
• Resolution: 2.597 Å
• Binding residue (original residue number in PDB): K191 D193 E194
• Binding residue (residue number reindexed from 1): K194 D196 E197
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): K166 K191 N192 D193 E194 H287 H321 K329
• Catalytic site (residue number reindexed from 1): K169 K194 N195 D196 E197 H290 H324 K332
• Enzyme Commision number: 4.1.1.39: ribulose-bisphosphate carboxylase.

Gene Ontology

Molecular Function

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

Biological Process

• GO:0015977 carbon fixation

External links

• PDB: RCSB:5c2g, PDBe:5c2g, PDBj:5c2g
• PDBsum: 5c2g
• PubMed: 26617072
• UniProt: A0A0X1KHE5