Structure of PDB 2amy Chain A

Receptor sequence
>2amyA (length=240) Species: 9606 (Homo sapiens) [Search protein sequence]
PGPALCLFDVDGTLTAPRQKITKEMDDFLQKLRQKIKIGVVGGSDFEKVQ
EQLGNDVVEKYDYVFPENGLVAYKDGKLLCRQNIQSHLGEALIQDLINYC
LSYIAKIKLPKKRGTFIEFRNGMLNVSPIGRSCSQEERIEFYELDKKENI
RQKFVADLRKEFAGKGLTFSIGGQISFDVFPDGWDKRYCLRHVENDGYKT
IYFFGDKTMNDHEIFTDPRTMGYSVTAPEDTRRICELLFS
3D structure
PDB2amy X-Ray Structure of Human Phosphomannomutase 2 (PMM2)
ChainA
Resolution2.09 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 GLY A K202 R225 K199 R219
BS02 GLY A F221 T222 D223 T226 G228 F215 T216 D217 T220 G222
BS03 GLY A Y102 S105 Y106 K109 Y99 S102 Y103 K106
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:0006486 protein glycosylation
GO:0006487 protein N-linked glycosylation
GO:0009298 GDP-mannose biosynthetic process
GO:0019309 mannose catabolic process
GO:0061728 GDP-mannose biosynthetic process from mannose
GO:0061729 GDP-mannose biosynthetic process from fructose-6-phosphate
GO:0141199 GDP-mannose biosynthetic process from glucose
Cellular Component
GO:0005654 nucleoplasm
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:2amy, PDBe:2amy, PDBj:2amy
PDBsum2amy
PubMed
UniProtO15305|PMM2_HUMAN Phosphomannomutase 2 (Gene Name=PMM2)

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