Structure of PDB 6aef Chain A

Receptor sequence
>6aefA (length=458) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
FSITTLRDWTPDPGSIICWHASPTAKAKARQAPISEVPPSYQQAQHLRRY
RDHVARGLDMSRLMIFTWDLPGRCNIRAMNYAINAHLRRHDTYHSWFEFD
NAEHIVRHTIADPADIEVVQAEHQNMTSAELRHHIATPQPLQWDCFLFGI
IQSDDHFTFYASIAHLCVDPMIVGVLFIEIHMMYSALVGGDPPIELPPAG
RYDDHCVRQYADTAALTLDSARVRRWVEFAANNDGTLPHFPLPLGDLSVP
HTGKLLTETLMDEQQGERFEAACVAAGARFSGGVFACAALAERELTNCET
FDVVTTTDTRRTPTELRTTGWFTGLVPITVPVASGLFDSAARVAQISFDS
GKDLATVPFDRVLELARPETGLRPPRPGNFVMSFLDASIAPLSTVANSDL
NFRIYDEGRVSHQVSMWVNRYQHQTTVTVLFPDNPIASESVANYIAAMKS
IYIRTADG
3D structure
PDB6aef A novel mutation alters the stability of PapA2 resulting in the complete abrogation of sulfolipids in clinical mycobacterial strains.
ChainA
Resolution2.16 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.288: 2-O-sulfo trehalose long-chain-acyltransferase.
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 ZN A C19 H21 H124 H135 C18 H20 H123 H134
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006629 lipid metabolic process
GO:0008610 lipid biosynthetic process
GO:0046506 sulfolipid biosynthetic process
GO:0071555 cell wall organization

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6aef, PDBe:6aef, PDBj:6aef
PDBsum6aef
PubMed
UniProtP9WIK7|PAPA2_MYCTU Trehalose-2-sulfate acyltransferase PapA2 (Gene Name=papA2)

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