Structure of PDB 5jzu Chain A

Receptor sequence
>5jzuA (length=429) Species: 9606 (Homo sapiens) [Search protein sequence]
KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI
3D structure
PDB5jzu Aspartate/asparagine-beta-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern.
ChainA
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.16: peptide-aspartate beta-dioxygenase.
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 peptide A L465 L466 F496 R526 F529 H530 Y565 D616 E617 Q664 K666 T680 P682 R686 R688 I758 L136 L137 F167 R197 F200 H201 Y236 D287 E288 Q335 K337 T351 P353 R357 R359 I429
BS02 MN A H679 H725 H350 H396
Gene Ontology
Molecular Function
GO:0062101 peptidyl-aspartic acid 3-dioxygenase activity
Biological Process
GO:0018193 peptidyl-amino acid modification
GO:0042264 peptidyl-aspartic acid hydroxylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5jzu, PDBe:5jzu, PDBj:5jzu
PDBsum5jzu
PubMed31659163
UniProtQ12797|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)

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