Structure of PDB 3i27 Chain D

Receptor sequence
>3i27D (length=369) Species: 360393 (Breda virus serotype 1) [Search protein sequence]
TPVTPYYGPGHITFDWCGFGDSRSDCTNPQSPMSLDIPQQLCPKFSSKSS
SSMFLSLHWNNHSSFVSYDYFNCGVEKVFYEGVNFSPRKQYSCWDEGVDG
WIELKTRFYTKLYQMATTSRCIKLIQLQAPSSLPTLQAGVCRTNKQLPDN
PRLALLSDTVPTSVQFVLPGSSGTTICTKHLVPFCYLNHGCFTTGGSCLP
FGVSYVSDSFYYGYYDATPQIGSTESHDYVCDYLFMEPGTYNASTVGKFL
VYPTKSYCMDTMNITVPVQAVQSIWSEQYASDDAIGQACKAPYCIFYNKT
TPYTVTNGSDANHGDDEVRMMMQGLLRNSSCISPQGSTPLALYSTEMIYE
PNYGSCPQFYKLFDTSGNE
3D structure
PDB3i27 Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases
ChainD
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.1.53: sialate O-acetylesterase.
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 MAN D A295 S296 A280 S281
BS02 SID D G154 V155 L170 F207 T208 T209 G210 E240 G139 V140 L155 F192 T193 T194 G195 E225
Gene Ontology
Molecular Function
GO:0001681 sialate O-acetylesterase activity
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0030246 carbohydrate binding
GO:0046789 host cell surface receptor binding
GO:0106330 sialate 9-O-acetylesterase activity
GO:0106331 sialate 4-O-acetylesterase activity
Biological Process
GO:0019064 fusion of virus membrane with host plasma membrane
GO:0044650 adhesion of symbiont to host cell
Cellular Component
GO:0016020 membrane
GO:0019031 viral envelope
GO:0020002 host cell plasma membrane
GO:0055036 virion membrane

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Molecular Function
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Cellular Component
External links
PDB RCSB:3i27, PDBe:3i27, PDBj:3i27
PDBsum3i27
PubMed19721004
UniProtP0C0V9|HEMA_BRV1 Hemagglutinin-esterase (Gene Name=HE)

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