Structure of PDB 4nhy Chain A Binding Site BS02

Receptor Information
>4nhy Chain A (length=461) 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
VPMCQGELRHWKTGHYTLIHDHSKAEFALDLILYCGCEGWEPEYGGFTSY
IAKGEDEELLTVNPESNSLALVYRDRETLKFVKHINHRSLEQKKTFPNRT
GFWDFSFIYYE
Ligand information
Ligand IDPD2
InChIInChI=1S/C7H5NO4/c9-6(10)4-1-2-8-5(3-4)7(11)12/h1-3H,(H,9,10)(H,11,12)
InChIKeyMJIVRKPEXXHNJT-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)c1ccnc(c1)C(O)=O
ACDLabs 10.04O=C(O)c1nccc(C(=O)O)c1
OpenEye OEToolkits 1.5.0c1cnc(cc1C(=O)O)C(=O)O
FormulaC7 H5 N O4
NamePYRIDINE-2,4-DICARBOXYLIC ACID
ChEMBLCHEMBL316034
DrugBank
ZINCZINC000000391915
PDB chain4nhy 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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PDB4nhy Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases.
Resolution2.603 Å
Binding residue
(original residue number in PDB)		L152 I167 L182 H218 V220 R230
Binding residue
(residue number reindexed from 1)		L129 I144 L159 H195 V197 R207
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=5.64,IC50=2.3uM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4nhy, PDBe:4nhy, PDBj:4nhy
PDBsum4nhy
PubMed25728928
UniProtQ8N543|OGFD1_HUMAN Prolyl 3-hydroxylase OGFOD1 (Gene Name=OGFOD1)

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