Structure of PDB 7yb8 Chain A Binding Site BS02
Receptor Information
>7yb8 Chain A (length=429) Species:
9606
(Homo sapiens) [
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KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
7yb8 Chain A Residue 1003 [
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Receptor-Ligand Complex Structure
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PDB
7yb8
Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with D-2-hydroxyglutarate and factor X-derived peptide (39mer-4Ser)
Resolution
1.98 Å
Binding residue
(original residue number in PDB)
H679 H725
Binding residue
(residue number reindexed from 1)
H350 H396
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.14.11.16
: peptide-aspartate beta-dioxygenase.
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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