Structure of PDB 4nhy Chain D Binding Site BS02

Receptor Information
>4nhy Chain D (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 D Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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 Y169 L182 H218 V220 R230 W236
Binding residue
(residue number reindexed from 1)		L129 I144 Y146 L159 H195 V197 R207 W213
Annotation score1
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
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Biological Process
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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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