Structure of PDB 4kvk Chain A
Receptor sequence
>4kvkA (length=611) Species:
4530
(Oryza sativa) [
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GSVHPDLRDVFSKMSFFDKIGFLFIHAFDKRNLWHKVPVPIGLLYLNTRR
TLLEKYNLLAVGRSSHGALFDPKEFLYRTEDGKYNDPHNAEAGSQNTFFG
RNMEPVDQQDELMSPDPFVVATKLLARREYKDTGKQFNILAAAWIQFMVH
DWMDHMEDTGQIGITAPKEVANECPLKSFKFHPTKELPTNSDGIKIGHYN
IRTAWWDGSAVYGNNEERAEKLRTYVDGKLVIGDDGLLLHKENGVALSGD
IRNSWAGVSILQALFVKEHNAVCDAIKEEHPNLSDEELYRYAKLVTSAVI
AKVHTIDWTVELLKTKTMRAAMRANWYGLLGKKIKDTFGHIGGPILGGLV
GLKKPNNHGVPYSLTEEFTSVYRMHSLIPSTLKLRDPTGQPDANNSPPCL
EDIDIGEMIGLKGEEQLSKIGFEKQALSMGYQACGALELWNYPSFFRNLI
PQNLDGTNRSDRIDLAALEVYRDRERSVPRYNEFRRRLFLIPIKSWEDLT
SDKDAIETIRAIYGDDVEKLDLLVGLMAEKKIKGFAISETAFNIFILMAS
RRLEADRFFTSNFNEETYTKKGMQWVKTTEGLRDVINRHYPEITAKWMKS
SSAFSVWDADY
3D structure
PDB
4kvk
Crystal structures of alpha-dioxygenase from Oryza sativa: Insights into substrate binding and activation by hydrogen peroxide.
Chain
A
Resolution
1.98 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 V156 H157 H162 N260 W262 T376 Y379 H382 I416 F453 L456 L472 L475 R479 R483
I145 Q146 V149 H150 H155 N253 W255 T369 Y372 H375 I409 F446 L449 L465 L468 R472 R476
BS02
DMU
A
S19 K20 S22 F23 F24
S12 K13 S15 F16 F17
BS03
CA
A
T210 W212 D214 S216
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:4kvk
,
PDBe:4kvk
,
PDBj:4kvk
PDBsum
4kvk
PubMed
23934749
UniProt
Q2QRV3
|PIOX_ORYSJ Alpha-dioxygenase PIOX (Gene Name=PIOX)
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