Structure of PDB 2fuc Chain A Binding Site BS02

Receptor Information
>2fuc Chain A (length=245) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAE
QLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINF
CLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEK
IREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFD
TIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFP
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2fuc Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fuc The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a.
Resolution2.1 Å
Binding residue
(original residue number in PDB)
F230 D232 T235
Binding residue
(residue number reindexed from 1)
F219 D221 T224
Annotation score1
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2fuc, PDBe:2fuc, PDBj:2fuc
PDBsum2fuc
PubMed16540464
UniProtQ92871|PMM1_HUMAN Phosphomannomutase 1 (Gene Name=PMM1)

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