Structure of PDB 6apl Chain E

Receptor sequence
>6aplE (length=285) Species: 9606 (Homo sapiens) [Search protein sequence]
CRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPALWDRLSQHKAPYGWR
GLSHQVIASTLSLLNGSESAKLFCIRCAVVGNGGILNGSRQGPNIDAHDY
VFRLNGAVIKGFERDVGTKTSFYGFTVNTMKNSLVSYWNLGFTSVPQGQD
LQYIFIPSDIRDYVMLRSAILGVPVPEGLDKGDRPHAYFGPEASASKFKL
LHPDFISYLTERFLKSKLINDLYMPSTGALMLLTALHTCDQVSAYGFITS
NYWKFSDHYFNHDLSLEAALWRDLHKAGILQLYQR
3D structure
PDB6apl Expression system for structural and functional studies of human glycosylation enzymes.
ChainE
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M302 H351
Catalytic site (residue number reindexed from 1) M224 H262
Enzyme Commision number 2.4.3.3: alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase.
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 C5P E N156 G157 L178 N179 S304 G306 F325 I326 D335 H336 N82 G83 L104 N105 S226 G228 F247 I248 D257 H258
Gene Ontology
Molecular Function
GO:0001665 alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity
GO:0008373 sialyltransferase activity
GO:0016757 glycosyltransferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0006493 protein O-linked glycosylation
GO:0016266 O-glycan processing
GO:0019082 viral protein processing
GO:1990743 protein sialylation
Cellular Component
GO:0000139 Golgi membrane
GO:0005794 Golgi apparatus
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6apl, PDBe:6apl, PDBj:6apl
PDBsum6apl
PubMed29251719
UniProtQ9UJ37|SIA7B_HUMAN Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (Gene Name=ST6GALNAC2)

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