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BioLiP

Structure of PDB 7bmi Chain A Binding Site BS01

Receptor Information
>7bmi Chain A (length=429) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY
GKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDR
QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEE
VLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYF
HLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPK
ETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT
LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPH
TGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQ
DASSFRLIFIVDVWHPELTPQQRRSLPAI
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7bmi Fluorinated derivatives of pyridine-2,4-dicarboxylate are potent inhibitors of human 2-oxoglutarate dependent oxygenases
Resolution1.66 Å
Binding residue
(original residue number in PDB)		A389 R393 S394 N395 F432 L433 L465 H493 F496 R526 F529 H530 Y565 E617 Q627 Q632 K666 T680 P682 R686 R688 I758
Binding residue
(residue number reindexed from 1)		A60 R64 S65 N66 F103 L104 L136 H164 F167 R197 F200 H201 Y236 E288 Q298 Q303 K337 T351 P353 R357 R359 I429
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

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Molecular Function
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Biological Process
External links
PDB RCSB:7bmi, PDBe:7bmi, PDBj:7bmi
PDBsum7bmi
PubMed
UniProtQ12797|ASPH_HUMAN Aspartyl/asparaginyl beta-hydroxylase (Gene Name=ASPH)

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