Structure of PDB 6yyy Chain A

Receptor sequence

>6yyyA (length=428) Species: 9606 (Homo sapiens) [Search protein sequence]

PKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYG
KAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQ
QFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEV
LSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFH
LGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKE
TGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTL
WQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHT
GPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQD
ASSFRLIFIVDVWHPELTPQQRRSLPAI

3D structure

PDB

6yyy Synthesis of 2-oxoglutarate derivatives and their evaluation as cosubstrates and inhibitors of human aspartate/asparagine-beta-hydroxylase.

Chain

Resolution

2.29 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)
BS01	peptide	A	R393 S394 N395 F432 L433 L466 H493 R526 H530 Y565 D616 E617 W625 Q632 Q664 T680 P682 R686 R688 I758	R63 S64 N65 F102 L103 L136 H163 R196 H200 Y235 D286 E287 W295 Q302 Q334 T350 P352 R356 R358 I428
BS02	MN	A	H679 H725	H349 H395
BS03	Q1W	A	W625 S668 M670 R688 H725 R735	W295 S338 M340 R358 H395 R405

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:6yyy, PDBe:6yyy, PDBj:6yyy
PDBsum	6yyy
PubMed	34163896
UniProt	Q12797\|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)

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