Structure of PDB 1vne Chain A

Receptor sequence
>1vneA (length=574) Species: 38902 (Curvularia inaequalis) [Search protein sequence]
VTPIPLPKIDEPEEYNTNYILFWNHVGLELNRVTHTVGGPLTGPPLSARA
LGMLHLAIHDAYFSICPPTDFTTFLSPDTENAAYRLPSPNGANDARQAVA
GAALKMLSSLYMKPVEQPNPNPGANISDNAYAQLGLVLDRSVLEAPGGVD
RESASFMFGEDVADVFFALLNDPRGASQEGYHPTPGRYKFDDEPTHPVVL
IPVDPNNPNGPKMPFRQYHAPFYGKTTKRFATQSEHFLADPPGLRSNADE
TAEYDDAVRVAIAMGGAQALNSTKRSPWQTAQGLYWAYAGSNLIGTPPRF
YNQIVRRIAVTYKKEEDLANSEVNNADFARLFALVDVACTDAGIFSWKEK
WEFEFWRPLSGVRDDGRPDHGDPFWLTLGAPATNTNDIPFKPPFPAYPSG
HATFGGAVFQMVRRYYNGRVGTWKDDEPDNIAIDMMISEELNGVNRDLRQ
PYDPTAPIEDQPGIVRTRIVRHFDSAWELMFENAISRIFLGVHWRFDAAA
ARDILIPTTTKDVYAVDNNGATVFQNVEDIRYTTRGTREDEEGLFPIGGV
PLGIEIADEIFNNGLKPTPPEIQP
3D structure
PDB1vne X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K353 R360 S402 G403 H404 R490 H496
Catalytic site (residue number reindexed from 1) K350 R357 S399 G400 H401 R487 H493
Enzyme Commision number 1.11.1.10: chloride peroxidase.
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 VO4 A K353 R360 S402 G403 H404 R490 H496 K350 R357 S399 G400 H401 R487 H493
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016691 chloride peroxidase activity
GO:0046872 metal ion binding
Biological Process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1vne, PDBe:1vne, PDBj:1vne
PDBsum1vne
PubMed10499093
UniProtP49053|PRXC_CURIN Vanadium chloroperoxidase (Gene Name=CPO)

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