Structure of PDB 5jtc Chain A Binding Site BS01
Receptor Information
>5jtc Chain A (length=429) Species:
9606
(Homo sapiens) [
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KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI
Ligand information
>5jtc Chain B (length=18) Species:
9606
(Homo sapiens) [
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GKCKDGLGEYTCTSLEGF
Receptor-Ligand Complex Structure
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PDB
5jtc
Aspartate/asparagine-beta-hydroxylase: a high-throughput mass spectrometric assay for discovery of small molecule inhibitors.
Resolution
2.24 Å
Binding residue
(original residue number in PDB)
A389 E390 R393 S394 N395 F432 L433 H493 F496 R526 F529 H530 Y565 D616 E617 T680 G681 P682 R686 R688 I758
Binding residue
(residue number reindexed from 1)
A60 E61 R64 S65 N66 F103 L104 H164 F167 R197 F200 H201 Y236 D287 E288 T351 G352 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
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:5jtc
,
PDBe:5jtc
,
PDBj:5jtc
PDBsum
5jtc
PubMed
32457455
UniProt
Q12797
|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)
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