Structure of PDB 3oka Chain B

Receptor sequence
>3okaB (length=378) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
SRKTLVVTNDFPPRIGGIQSYLRDFIATQDPESIVVFASTQNAEEAHAYD
KTLDYEVIRWPRSVMLPTPTTAHAMAEIIREREIDNVWFGAAAPLALMAG
TAKQAGASKVIASTHGHEVGWSMLPGSRQSLRKIGTEVDVLTYISQYTLR
RFKSAFGSHPTFEHLPSGVDVKRFTPATPEDKSATRKKLGFTDTTPVIAC
NSRLVPRKGQDSLIKAMPQVIAARPDAQLLIVGSGRYESTLRRLATDVSQ
NVKFLGRLEYQDMINTLAAADIFAMPARTRGGGLDVEGLGIVYLEAQACG
VPVIAGTSGGAPETVTPATGLVVEGSDVDKLSELLIELLDDPIRRAAMGA
AGRAHVEAEWSWEIMGERLTNILQSEPR
3D structure
PDB3oka Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB'.
ChainB
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.346: phosphatidyl-myo-inositol dimannoside synthase.
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 R206 K211 R260 L261 M266 E298 R203 K208 R257 L258 M263 E295 MOAD: Kd=19uM
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
GO:0033164 glycolipid 1,6-alpha-mannosyltransferase activity
GO:0043750 phosphatidylinositol alpha-mannosyltransferase activity
Biological Process
GO:0008654 phospholipid biosynthetic process
GO:0009247 glycolipid biosynthetic process
GO:0046488 phosphatidylinositol metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3oka, PDBe:3oka, PDBj:3oka
PDBsum3oka
PubMed20843801
UniProtQ8NNK8|PIMB_CORGL GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase (Gene Name=pimB)

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