Structure of PDB 5nfo Chain B Binding Site BS02
Receptor Information
>5nfo Chain B (length=318) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
SHMAEAALEAVRSELREFPAAARELCVPLAVPYLDKPPTPLHFYRDWVCP
NRPCIIRNALQHWPALQKWSLPYFRATVGSTEVSVAVTPDGYADAVRGDR
FMMPAERRLPLSFVLDVLEGRAQHPGVLYVQKQCSNLPSELPQLLPDLES
HVPWASEALGKMPDAVNFWLGEAAAVTSLHKDHYENLYCVVSGEKHFLFH
PPSDRPFIPYELYTPATYQLTEEGTFKVVDEEAMEKVPWIPLDPLAPDLA
RYPSYSQAQALCCTVRAGEMLYLPALWFHHVQQSQGCIAVNFWYDMEYDL
KYSYFQLLDSLTKASGLD
Ligand information
Ligand ID
AKG
InChI
InChI=1S/C5H6O5/c6-3(5(9)10)1-2-4(7)8/h1-2H2,(H,7,8)(H,9,10)
InChIKey
KPGXRSRHYNQIFN-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=C(O)C(=O)CCC(=O)O
OpenEye OEToolkits 1.7.6
C(CC(=O)O)C(=O)C(=O)O
CACTVS 3.385
OC(=O)CCC(=O)C(O)=O
Formula
C5 H6 O5
Name
2-OXOGLUTARIC ACID
ChEMBL
CHEMBL1686
DrugBank
DB08845
ZINC
ZINC000001532519
PDB chain
5nfo Chain B Residue 502 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
5nfo
(3S)-Lysyl hydroxylation of TRAFAC GTPases is catalyzed by the human Jumonji-C oxygenase JMJD7.
Resolution
2.173 Å
Binding residue
(original residue number in PDB)
Y127 W167 T175 H178 N184 Y186 H277 V279 W291
Binding residue
(residue number reindexed from 1)
Y129 W169 T177 H180 N186 Y188 H279 V281 W293
Annotation score
5
Enzymatic activity
Enzyme Commision number
1.14.11.63
: peptidyl-lysine (3S)-dioxygenase.
3.4.-.-
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:5nfo
,
PDBe:5nfo
,
PDBj:5nfo
PDBsum
5nfo
PubMed
UniProt
P0C870
|JMJD7_HUMAN Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7 (Gene Name=JMJD7)
[
Back to BioLiP
]