Structure of PDB 8goa Chain C

Receptor sequence

>8goaC (length=367) Species: 83333 (Escherichia coli K-12)

MDRIIQSPGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEK
SFKDAGLVVEIAPFGGECSQNEIDRLRGIAETAQCGAILGIGGGKTLDTA
KALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMV
IVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAGGKCTQAAL
ALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFESGGL
AAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALS
HAVGLPITLAQLDIKEDVPAKMRIVAEAACAEGETIHNMPGGATPDQVYA
ALLVADQYGQRFLQEWE

3D structure

• PDB: 8goa Structural and functional insights into the flexible beta-hairpin of glycerol dehydrogenase.
• Chain: C
• Resolution: 2.9 Å

Enzymatic activity

• Enzyme Commision number: 1.1.1.6: glycerol dehydrogenase.
  1.1.1.75: (R)-aminopropanol dehydrogenase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	C	D171 H254 H271	D171 H254 H271

Gene Ontology

Molecular Function

• GO:0008270 zinc ion binding
• GO:0008888 glycerol dehydrogenase (NAD+) activity
• GO:0016491 oxidoreductase activity
• GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
• GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
• GO:0019147 (R)-aminopropanol dehydrogenase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006071 glycerol metabolic process
• GO:0019588 anaerobic glycerol catabolic process
• GO:0051289 protein homotetramerization
• GO:0051596 methylglyoxal catabolic process

Cellular Component

• GO:0005829 cytosol
• GO:0032991 protein-containing complex

External links

• PDB: RCSB:8goa, PDBe:8goa, PDBj:8goa
• PDBsum: 8goa
• PubMed: 37165682
• UniProt: P0A9S5|GLDA_ECOLI Glycerol dehydrogenase (Gene Name=gldA)