Structure of PDB 2fuc Chain A

Receptor sequence
>2fucA (length=245) Species: 9606 (Homo sapiens) [Search protein sequence]
ERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAE
QLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINF
CLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEK
IREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFD
TIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFP
3D structure
PDB2fuc The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a.
ChainA
Resolution2.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MG A D19 D21 N218 D8 D10 N207
BS02 MG A F230 D232 T235 F219 D221 T224
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

View graph for
Molecular Function

View graph for
Biological Process

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

[Back to BioLiP]