Structure of PDB 7e6j Chain A

Receptor sequence
>7e6jA (length=429) Species: 9606 (Homo sapiens) [Search protein sequence]
KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEAEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI
3D structure
PDB7e6j Human Oxygenase Variants Employing a Single Protein Fe II Ligand Are Catalytically Active.
ChainA
Resolution1.9 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 R393 S394 N395 Q431 F432 L433 G434 M436 L465 H493 F496 R526 F529 H530 L564 Y565 D616 E617 Q627 K666 P682 R686 R688 I758 R64 S65 N66 Q102 F103 L104 G105 M107 L136 H164 F167 R197 F200 H201 L235 Y236 D287 E288 Q298 K337 P353 R357 R359 I429
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:7e6j, PDBe:7e6j, PDBj:7e6j
PDBsum7e6j
PubMed33887099
UniProtQ12797|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)

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