Structure of PDB 5iax Chain A

Receptor sequence
>5iaxA (length=199) Species: 1392 (Bacillus anthracis) [Search protein sequence]
EQTIFDHKGNVIKTEDREIQIISKFEEPLIVVLGNVLSDEECDELIELSK
SKLARSKVDVNDIAFLDDNELTAKIEKRISSIMNVPASHGEGLHILNYEV
DQQYKAHYDYFAEHSRSAANNRISTLVMYLNDVEEGGETFFPKLNLSVHP
RKGMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQWVRRGTYKPPG
3D structure
PDB5iax Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns.
ChainA
Resolution2.1 Å
3D
structure
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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 CO A H127 D129 H193 H107 D109 H173
BS02 AKG A Y118 Y124 H127 D129 T159 H193 K203 I205 T207 W209 Y98 Y104 H107 D109 T139 H173 K183 I185 T187 W189
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5iax, PDBe:5iax, PDBj:5iax
PDBsum5iax
PubMed27129244
UniProtA0A4Y1WAP5

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