Structure of PDB 7ybc Chain A

Receptor sequence

>7ybcA (length=429) Species: 9606 (Homo sapiens)

KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI

3D structure

• PDB: 7ybc Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with (S)-4-hydroxy-4-methyl-2-oxoglutarate and factor X-derived peptide (39mer-4Ser)
• Chain: A
• Resolution: 1.84 Å

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	A389 R393 S394 N395 Q431 F432 L433 G434 M436 H493 F496 R526 F529 H530 L564 Y565 E617 K666 P682 R686 R688 I758	A60 R64 S65 N66 Q102 F103 L104 G105 M107 H164 F167 R197 F200 H201 L235 Y236 E288 K337 P353 R357 R359 I429
BS02	MN	A	H679 H725	H350 H396
BS03	IOW	A	W625 S668 M670 H679 R688 H690 H725 R735 I739	W296 S339 M341 H350 R359 H361 H396 R406 I410

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

External links

• PDB: RCSB:7ybc, PDBe:7ybc, PDBj:7ybc
• PDBsum: 7ybc
• UniProt: Q12797|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)