Structure of PDB 2fuc Chain A Binding Site BS02
Receptor Information
>2fuc Chain A (length=245) Species:
9606
(Homo sapiens) [
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ERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAE
QLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINF
CLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEK
IREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFD
TIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFP
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
2fuc Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
2fuc
The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
F230 D232 T235
Binding residue
(residue number reindexed from 1)
F219 D221 T224
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
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Molecular Function
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Cellular Component
External links
PDB
RCSB:2fuc
,
PDBe:2fuc
,
PDBj:2fuc
PDBsum
2fuc
PubMed
16540464
UniProt
Q92871
|PMM1_HUMAN Phosphomannomutase 1 (Gene Name=PMM1)
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