Structure of PDB 4nhy Chain C

Receptor sequence
>4nhyC (length=457) Species: 9606 (Homo sapiens) [Search protein sequence]
AEFSDAVTEETLKKQVAEAWSRRTPFSHEVIVMDMDPFLHCVIPNFIQSQ
DFLEGLQKELMNLDFHEKYNDLYKFQQSDDLKKRREPHISTLRKILFEDF
RSWLSDISKIDLESTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPP
WDRSMGGTLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSPVSFHQVSEV
LSEEKSRLSISGWFHGPSLTRPPNYFEPPIPRSPHIPQDHEILYDWINPT
YLDMDYQVQIQEEFEESSEILLKEFLKPEKFTKVCEALEHGHVEWSSRGP
PNKRFYEKAEESKLPEILKECMKLFRSEALFLLLSNFTGLKLHFLAPSSV
PMCQGELRHWKTGHYTLIHKAEFALDLILYCGCEGWEPEYGGFTSYIAKG
EDEELLTVNPESNSLALVYRDRETLKFVKHINHRSLEQKKTFPNRTGFWD
FSFIYYE
3D structure
PDB4nhy Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases.
ChainC
Resolution2.603 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.-
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 C H155 D157 H218 H132 D134 H195
BS02 PD2 C L152 D157 I167 L182 H218 V220 R230 L129 D134 I144 L159 H195 V197 R207
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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