Structure of PDB 5jzu Chain A Binding Site BS01

Receptor Information
>5jzu Chain A (length=429) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5jzu Aspartate/asparagine-beta-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		L465 L466 F496 R526 F529 H530 Y565 D616 E617 Q664 K666 T680 P682 R686 R688 I758
Binding residue
(residue number reindexed from 1)		L136 L137 F167 R197 F200 H201 Y236 D287 E288 Q335 K337 T351 P353 R357 R359 I429
Enzymatic activity
Enzyme Commision number 1.14.11.16: peptide-aspartate beta-dioxygenase.
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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