Structure of PDB 2glx Chain C Binding Site BS01

Receptor Information

>2glx Chain C (length=332) Species: 106592 (Ensifer adhaerens)

NRWGLIGASTIAREWVIGAIRATGGEVVSMMSTSAERGAAYATENGIGKS
VTSVEELVGDPDVDAVYVSTTNELHREQTLAAIRAGKHVLCEKPLAMTLE
DAREMVVAAREAGVVLGTNHHLRNAAAHRAMRDAIAEGRIGRPIAARVFH
AVYLPPHLQGWRLERPEAGGGVILDITVHDADTLRFVLNDDPAEAVAISH
SAGMGKEGVEDGVMGVLRFQSGVIAQFHDAFTTKFAETGFEVHGTEGSLI
GRNVMTQKPVGTVTLRNAEGESQLPLDPANLYETALAAFHSAIEGHGQPS
ATGEDGVWSLATGLAVVKAAATGQAAEIETGL

Ligand information

• Ligand ID: ACT
• InChI: InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
• InChIKey: QTBSBXVTEAMEQO-UHFFFAOYSA-M
• SMILES:
  ACDLabs 10.04: [O-]C(=O)C
  OpenEye OEToolkits 1.5.0: CC(=O)[O-]
  CACTVS 3.341: CC([O-])=O
• Formula: C2 H3 O2
• Name: ACETATE ION
• DrugBank: DB14511
• PDB chain: 2glx Chain C Residue 3502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2glx Crystal Structure of NADP(H)-Dependent 1,5-Anhydro-d-fructose Reductase from Sinorhizobium morelense at 2.2 A Resolution: Construction of a NADH-Accepting Mutant and Its Application in Rare Sugar Synthesis
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): K94 H122 H180 Q258
• Binding residue (residue number reindexed from 1): K93 H121 H179 Q257
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): K94 H180
• Catalytic site (residue number reindexed from 1): K93 H179
• Enzyme Commision number: 1.1.1.292: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming).

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0016491 oxidoreductase activity
• GO:0033712 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity

External links

• PDB: RCSB:2glx, PDBe:2glx, PDBj:2glx
• PDBsum: 2glx
• PubMed: 16906761
• UniProt: Q2I8V6|AFR_ENSAD 1,5-anhydro-D-fructose reductase (Gene Name=afr)