Structure of PDB 7ybb Chain A Binding Site BS01
Receptor Information
>7ybb Chain A (length=429) Species:
9606
(Homo sapiens) [
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KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI
Ligand information
>7ybb Chain B (length=18) Species:
32630
(synthetic construct) [
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GKCKDGLGEYTCTSLEGF
Receptor-Ligand Complex Structure
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PDB
7ybb
Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with D-4-hydroxy-2-oxoglutarate and factor X-derived peptide (39mer-4Ser)
Resolution
1.68 Å
Binding residue
(original residue number in PDB)
A389 R393 N395 Q431 F432 L433 M436 H493 F496 R526 F529 H530 Y565 E617 Q632 Q633 K666 T680 P682 R686 R688 I758
Binding residue
(residue number reindexed from 1)
A60 R64 N66 Q102 F103 L104 M107 H164 F167 R197 F200 H201 Y236 E288 Q303 Q304 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:7ybb
,
PDBe:7ybb
,
PDBj:7ybb
PDBsum
7ybb
PubMed
UniProt
Q12797
|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)
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