Structure of PDB 2fue Chain A Binding Site BS02

Receptor Information

>2fue Chain A (length=246) Species: 9606 (Homo sapiens)

RVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQ
LGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFC
LSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKI
REKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFDT
IHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFPET

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: 2fue Chain A Residue 500

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2fue The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a.
• Resolution: 1.75 Å
• Binding residue (original residue number in PDB): D19 D21 N218
• Binding residue (residue number reindexed from 1): D7 D9 N206
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 5.4.2.8: phosphomannomutase.

Gene Ontology

Molecular Function

• GO:0004615 phosphomannomutase activity
• GO:0005515 protein binding
• GO:0016853 isomerase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006013 mannose metabolic process
• GO:0006487 protein N-linked glycosylation
• GO:0009298 GDP-mannose biosynthetic process
• GO:1990830 cellular response to leukemia inhibitory factor

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0043025 neuronal cell body

External links

• PDB: RCSB:2fue, PDBe:2fue, PDBj:2fue
• PDBsum: 2fue
• PubMed: 16540464
• UniProt: Q92871|PMM1_HUMAN Phosphomannomutase 1 (Gene Name=PMM1)