Structure of PDB 5nfn Chain D

Receptor sequence
>5nfnD (length=318) Species: 9606 (Homo sapiens) [Search protein sequence]
SHMAEAALEAVRSELREFPAAARELCVPLAVPYLDKPPTPLHFYRDWVCP
NRPCIIRNALQHWPALQKWSLPYFRATVGSTEVSVAVTPDGYADAVRGDR
FMMPAERRLPLSFVLDVLEGRAQHPGVLYVQKQCSNLPSELPQLLPDLES
HVPWASEALGKMPDAVNFWLGEAAAVTSLHKDHYENLYCVVSGEKHFLFH
PPSDRPFIPYELYTPATYQLTEEGTFKVVDEEAMEKVPWIPLDPLAPDLA
RYPSYSQAQALRCTVRAGEMLYLPALWFHHVQQSQGCIAVNFWYDMEYDL
KYSYFQLLDSLTKASGLD
3D structure
PDB5nfn (3S)-Lysyl hydroxylation of TRAFAC GTPases is catalyzed by the human Jumonji-C oxygenase JMJD7.
ChainD
Resolution2.982 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.63: peptidyl-lysine (3S)-dioxygenase.
3.4.-.-
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 D H178 D180 H277 H180 D182 H279
BS02 AKG D Y127 W167 T175 H178 D180 N184 Y186 H277 V279 Y129 W169 T177 H180 D182 N186 Y188 H279 V281
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004177 aminopeptidase activity
GO:0004497 monooxygenase activity
GO:0005515 protein binding
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0035064 methylated histone binding
GO:0046872 metal ion binding
GO:0106155 peptidyl-lysine 3-dioxygenase activity
Biological Process
GO:0006508 proteolysis
GO:0018126 protein hydroxylation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5nfn, PDBe:5nfn, PDBj:5nfn
PDBsum5nfn
PubMed
UniProtP0C870|JMJD7_HUMAN Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7 (Gene Name=JMJD7)

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