Structure of PDB 1s3i Chain A Binding Site BS02

Receptor Information

>1s3i Chain A (length=307) Species: 10116 (Rattus norvegicus)

MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKADPDGLEAEKDG
VPVFKFPRWRARGQALPEVVAKYQALGAELNVLPFCSQFIPMEVINAPRH
GSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQK
ECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGTAPRCPQSEEGATY
EGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACGQKLTFFNSTLN
TSGLSTQGEALPIPGAHRPGVVTKAGLILFGNDDRMLLVKNIQLEDGKMM
PASQFFK

Ligand information

• Ligand ID: BME
• InChI: InChI=1S/C2H6OS/c3-1-2-4/h3-4H,1-2H2
• InChIKey: DGVVWUTYPXICAM-UHFFFAOYSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: C(CS)O
  ACDLabs 10.04
  CACTVS 3.341: OCCS
• Formula: C2 H6 O S
• Name: BETA-MERCAPTOETHANOL
• ChEMBL: CHEMBL254951
• DrugBank: DB03345
• ZINC: ZINC000008216595
• PDB chain: 1s3i Chain A Residue 315

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1s3i The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain.
• Resolution: 2.3 Å
• Binding residue (original residue number in PDB): T31 I32 F56 W59 C86
• Binding residue (residue number reindexed from 1): T31 I32 F56 W59 C86
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H106 D142
• Catalytic site (residue number reindexed from 1): H106 D142
• Enzyme Commision number: 1.5.1.6: formyltetrahydrofolate dehydrogenase.

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity

Biological Process

• GO:0009058 biosynthetic process

External links

• PDB: RCSB:1s3i, PDBe:1s3i, PDBj:1s3i
• PDBsum: 1s3i
• PubMed: 14729668
• UniProt: P28037|AL1L1_RAT Cytosolic 10-formyltetrahydrofolate dehydrogenase (Gene Name=Aldh1l1)