Structure of PDB 5jz6 Chain A

Receptor sequence
>5jz6A (length=429) Species: 9606 (Homo sapiens) [Search protein sequence]
KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI
3D structure
PDB5jz6 Aspartate/asparagine-beta-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern.
ChainA
Resolution2.354 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MN A H679 H725 H350 H396
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
View graph for
Biological Process
External links
PDB RCSB:5jz6, PDBe:5jz6, PDBj:5jz6
PDBsum5jz6
PubMed31659163
UniProtQ12797|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)

[Back to BioLiP]