Structure of PDB 4nhx Chain A Binding Site BS02

Receptor Information
>4nhx Chain A (length=457) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AEFSDAVTEETLKKQVAEAWSRRTPFSHEVIVMDMDPFLHCVIPNFIQSQ
DFLEGLQKELMNLDFHEKYNDLYKFQQSDDLKKRREPHISTLRKILFEDF
RSWLSDISKIDLESTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPP
WDRSMGGTLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSPVSFHQVSEV
LSEEKSRLSISGWFHGPSLTRPPNYFEPPIPRSPHIPQDHEILYDWINPT
YLDMDYQVQIQEEFEESSEILLKEFLKPEKFTKVCEALEHGHVEWSSRGP
PNKRFYEKAEESKLPEILKECMKLFRSEALFLLLSNFTGLKLHFLAPSSS
VPMCQGELRHWKTGHYTLIHAEFALDLILYCGCEGWEPEYGGFTSYIAKG
EDEELLTVNPESNSLALVYRDRETLKFVKHINHRSLEQKKTFPNRTGFWD
FSFIYYE
Ligand information
Ligand IDOGA
InChIInChI=1S/C4H5NO5/c6-2(7)1-5-3(8)4(9)10/h1H2,(H,5,8)(H,6,7)(H,9,10)
InChIKeyBIMZLRFONYSTPT-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)CNC(=O)C(O)=O
ACDLabs 10.04O=C(O)C(=O)NCC(=O)O
OpenEye OEToolkits 1.5.0C(C(=O)O)NC(=O)C(=O)O
FormulaC4 H5 N O5
NameN-OXALYLGLYCINE
ChEMBLCHEMBL90852
DrugBank
ZINCZINC000001534133
PDB chain4nhx Chain A Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4nhx Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases.
Resolution2.105 Å
Binding residue
(original residue number in PDB)		L152 H155 I167 Y169 H218 V220 R230
Binding residue
(residue number reindexed from 1)		L129 H132 I144 Y146 H195 V197 R207
Annotation score2
Binding affinityPDBbind-CN: -logKd/Ki=5.72,IC50=1.9uM
Enzymatic activity
Enzyme Commision number 1.14.11.-
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0031418 L-ascorbic acid binding
GO:0031543 peptidyl-proline dioxygenase activity
GO:0031544 peptidyl-proline 3-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0006449 regulation of translational termination
GO:0008283 cell population proliferation
GO:0018126 protein hydroxylation
GO:0019511 peptidyl-proline hydroxylation
GO:0034063 stress granule assembly
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0010494 cytoplasmic stress granule

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4nhx, PDBe:4nhx, PDBj:4nhx
PDBsum4nhx
PubMed25728928
UniProtQ8N543|OGFD1_HUMAN Prolyl 3-hydroxylase OGFOD1 (Gene Name=OGFOD1)

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