Structure of PDB 7ybb Chain A

Receptor sequence

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

KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI

3D structure

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)

Chain

Resolution

1.68 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	A389 R393 N395 Q431 F432 L433 M436 H493 F496 R526 F529 H530 Y565 E617 Q632 Q633 K666 T680 P682 R686 R688 I758	A60 R64 N66 Q102 F103 L104 M107 H164 F167 R197 F200 H201 Y236 E288 Q303 Q304 K337 T351 P353 R357 R359 I429
BS02	MN	A	H679 H725	H350 H396
BS03	IO9	A	W625 S668 H679 R688 H690 H725 R735 I737	W296 S339 H350 R359 H361 H396 R406 I408

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

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