Structure of PDB 7bmj Chain C

Receptor sequence
>7bmjC (length=428) Species: 9606 (Homo sapiens) [Search protein sequence]
PKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYG
KAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQ
QFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEV
LSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFH
LGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKE
TGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTL
WQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHT
GPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQD
ASSFRLIFIVDVWHPELTPQQRRSLPAI
3D structure
PDB7bmj Fluorinated derivatives of pyridine-2,4-dicarboxylate are potent inhibitors of human 2-oxoglutarate dependent oxygenases
ChainC
Resolution1.75 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)
Binding affinity
BS01 MN C H679 H725 H349 H395
BS02 U4Q C W625 S668 M670 H679 R688 H690 H725 V727 R735 W295 S338 M340 H349 R358 H360 H395 V397 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:7bmj, PDBe:7bmj, PDBj:7bmj
PDBsum7bmj
PubMed
UniProtQ12797|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)

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