Structure of PDB 6yyy Chain A Binding Site BS01
Receptor Information
>6yyy Chain A (length=428) Species:
9606
(Homo sapiens) [
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PKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYG
KAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQ
QFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEV
LSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFH
LGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKE
TGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTL
WQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHT
GPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQD
ASSFRLIFIVDVWHPELTPQQRRSLPAI
Ligand information
>6yyy Chain B (length=18) Species:
9606
(Homo sapiens) [
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GKCKDGLGEYTCTSLEGF
Receptor-Ligand Complex Structure
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PDB
6yyy
Synthesis of 2-oxoglutarate derivatives and their evaluation as cosubstrates and inhibitors of human aspartate/asparagine-beta-hydroxylase.
Resolution
2.29 Å
Binding residue
(original residue number in PDB)
R393 S394 N395 F432 L433 L466 H493 R526 H530 Y565 D616 E617 W625 Q632 Q664 T680 P682 R686 R688 I758
Binding residue
(residue number reindexed from 1)
R63 S64 N65 F102 L103 L136 H163 R196 H200 Y235 D286 E287 W295 Q302 Q334 T350 P352 R356 R358 I428
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:6yyy
,
PDBe:6yyy
,
PDBj:6yyy
PDBsum
6yyy
PubMed
34163896
UniProt
Q12797
|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)
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