Structure of PDB 4kvj Chain A

Receptor sequence
>4kvjA (length=611) Species: 4530 (Oryza sativa) [Search protein sequence]
GSVHPDLRDVFSKMSFFDKIGFLFIHAFDKRNLWHKVPVPIGLLYLNTRR
TLLEKYNLLAVGRSSHGALFDPKEFLYRTEDGKYNDPHNAEAGSQNTFFG
RNMEPVDQQDELMSPDPFVVATKLLARREYKDTGKQFNILAAAWIQFMVH
DWMDHMEDTGQIGITAPKEVANECPLKSFKFHPTKELPTNSDGIKIGHYN
IRTAWWDGSAVYGNNEERAEKLRTYVDGKLVIGDDGLLLHKENGVALSGD
IRNSWAGVSILQALFVKEHNAVCDAIKEEHPNLSDEELYRYAKLVTSAVI
AKVHTIDWTVELLKTKTMRAAMRANWYGLLGKKIKDTFGHIGGPILGGLV
GLKKPNNHGVPYSLTEEFTSVYRMHSLIPSTLKLRDPTGQPDANNSPPCL
EDIDIGEMIGLKGEEQLSKIGFEKQALSMGYQACGALELWNYPSFFRNLI
PQNLDGTNRSDRIDLAALEVYRDRERSVPRYNEFRRRLFLIPIKSWEDLT
SDKDAIETIRAIYGDDVEKLDLLVGLMAEKKIKGFAISETAFNIFILMAS
RRLEADRFFTSNFNEETYTKKGMQWVKTTEGLRDVINRHYPEITAKWMKS
SSAFSVWDADY
3D structure
PDB4kvj Crystal structures of alpha-dioxygenase from Oryza sativa: Insights into substrate binding and activation by hydrogen peroxide.
ChainA
Resolution2.12 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q153 H157 V378 Y379 H382 N550
Catalytic site (residue number reindexed from 1) Q146 H150 V371 Y372 H375 N543
Enzyme Commision number 1.13.11.92: fatty acid alpha-dioxygenase.
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 HEM A I152 Q153 H162 N260 W262 T376 Y379 H382 I416 F453 L472 L475 R479 R483 I145 Q146 H155 N253 W255 T369 Y372 H375 I409 F446 L465 L468 R472 R476
BS02 DMU A S19 K20 S22 F23 S12 K13 S15 F16
BS03 CA A D158 T210 W212 D214 S216 D151 T203 W205 D207 S209
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016491 oxidoreductase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0001561 fatty acid alpha-oxidation
GO:0006631 fatty acid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0006952 defense response
GO:0006979 response to oxidative stress
GO:0009627 systemic acquired resistance
GO:0009737 response to abscisic acid
GO:0009751 response to salicylic acid
GO:0031408 oxylipin biosynthetic process
GO:0034614 cellular response to reactive oxygen species
GO:0042742 defense response to bacterium
GO:0050832 defense response to fungus
GO:0071446 cellular response to salicylic acid stimulus
GO:0071732 cellular response to nitric oxide
GO:0098869 cellular oxidant detoxification
GO:1902609 (R)-2-hydroxy-alpha-linolenic acid biosynthetic process
Cellular Component
GO:0012511 monolayer-surrounded lipid storage body

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4kvj, PDBe:4kvj, PDBj:4kvj
PDBsum4kvj
PubMed23934749
UniProtQ2QRV3|PIOX_ORYSJ Alpha-dioxygenase PIOX (Gene Name=PIOX)

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