Structure of PDB 2wvm Chain B

Receptor sequence
>2wvmB (length=372) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]
MRLEIPNHTERFGVVRLHEVQRILELDSGRVRDESPAVGLRRLDDADLRD
VLEQTAIVVPTRNERLKLLEGVLSGIPHEALILVASNSSPDRFQMERDLL
EEFAHLTERPALIFHQKDPALAEALRAGGYPHPIGEDGLVRSGKAEGMIL
ALVFAALSGRRYVGFIDADNYFPGAVWEYVRAYAAGFLMAKTPFAMVRIL
WRRRYGRVSERNNRALNQLIGGVSGFETDVVKTANAGEHAMSLGLALRLP
LASGYAVEPQELVSLLELYGGVFPLEDEEVLQHGVEIFQIETRNPALHEN
KGDEHIRDMLLACLATVYHSKLATEEVRQSVLEELQAAEEPPPPVLYPPL
SSLDLQAVRKALRGHFSRFRVP
3D structure
PDB2wvm Structural Analysis of Thermus Thermophilus Hb27 Mannosyl-3-Phosphoglycerate Synthase Provides Evidence for a Second Catalytic Metal Ion and New Insight Into the Retaining Mechanism of Glycosyltransferases.
ChainB
Resolution2.977 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.-
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 GDD B P60 R62 E64 N87 Q116 G143 K144 D167 A168 D169 G250 Y268 E271 P60 R62 E64 N87 Q116 G143 K144 D167 A168 D169 G237 Y255 E258
BS02 ZN B H8 E19 D242 H8 E19 D229
BS03 ZN B E292 H296 E279 H283
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
GO:0046872 metal ion binding
GO:0050504 mannosyl-3-phosphoglycerate synthase activity
Biological Process
GO:0051479 mannosylglycerate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2wvm, PDBe:2wvm, PDBj:2wvm
PDBsum2wvm
PubMed20356840
UniProtQ72K30

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