Structure of PDB 7yb8 Chain A

Receptor sequence

>7yb8A (length=429) Species: 9606 (Homo sapiens) [Search protein sequence]

KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI

3D structure

PDB

7yb8 Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with D-2-hydroxyglutarate and factor X-derived peptide (39mer-4Ser)

Chain

Resolution

1.98 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	E390 R393 S394 N395 F432 L433 H493 F496 R526 F529 H530 L564 Y565 D616 E617 Q632 Q633 K666 P682 R686 R688 I758	E61 R64 S65 N66 F103 L104 H164 F167 R197 F200 H201 L235 Y236 D287 E288 Q303 Q304 K337 P353 R357 R359 I429
BS02	MN	A	H679 H725	H350 H396
BS03	2HG	A	W625 S668 M670 H679 R688 H690 F719 H725 R735	W296 S339 M341 H350 R359 H361 F390 H396 R406

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:7yb8, PDBe:7yb8, PDBj:7yb8
PDBsum	7yb8
PubMed
UniProt	Q12797\|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)

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