Structure of PDB 2fue Chain A

Receptor sequence
>2fueA (length=246) Species: 9606 (Homo sapiens) [Search protein sequence]
RVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQ
LGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFC
LSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKI
REKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFDT
IHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFPET
3D structure
PDB2fue The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a.
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.4.2.8: phosphomannomutase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 M1P A R28 R132 R143 R150 G185 M186 I187 S188 D190 R16 R120 R131 R138 G173 M174 I175 S176 D178
BS02 MG A D19 D21 N218 D7 D9 N206
BS03 MG A F230 D232 T235 F218 D220 T223
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:2fue, PDBe:2fue, PDBj:2fue
PDBsum2fue
PubMed16540464
UniProtQ92871|PMM1_HUMAN Phosphomannomutase 1 (Gene Name=PMM1)

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