Structure of PDB 5hv0 Chain B

Receptor sequence
>5hv0B (length=197) Species: 1392 (Bacillus anthracis) [Search protein sequence]
NNNQIGENKEQTIFDHKGNVIKTEDREIQIISKFEEPLIVVLGNVLSDEE
CDELIELSKSKLSGAFLDDNELTAKIEKRISSIMNVPASHGEGLHILNYE
VDQQYKAHYDYFAEHSRSAANNRISTLVMYLNDVEEGGETFFPKLNLSVH
PRKGMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQWVRRGTYK
3D structure
PDB5hv0 Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis.
ChainB
Resolution1.63 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number ?
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 CD B H127 D129 H193 H108 D110 H174
BS02 CD B E119 E202 E100 E183
BS03 AKG B Y118 H127 T159 K203 I205 T207 W209 Y99 H108 T140 K184 I186 T188 W190 MOAD: Kd=1.1uM
Gene Ontology
Molecular Function
GO:0003674 molecular_function
GO:0004656 procollagen-proline 4-dioxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0031418 L-ascorbic acid binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0008150 biological_process
GO:0018401 peptidyl-proline hydroxylation to 4-hydroxy-L-proline

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5hv0, PDBe:5hv0, PDBj:5hv0
PDBsum5hv0
PubMed27139630
UniProtA0A4Y1WAP5

[Back to BioLiP]