Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4KVK

Crystal structure of Oryza sativa fatty acid alpha-dioxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001561biological_processfatty acid alpha-oxidation
A0004601molecular_functionperoxidase activity
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006952biological_processdefense response
A0006979biological_processresponse to oxidative stress
A0009627biological_processsystemic acquired resistance
A0009737biological_processresponse to abscisic acid
A0009751biological_processresponse to salicylic acid
A0012511cellular_componentmonolayer-surrounded lipid storage body
A0016491molecular_functionoxidoreductase activity
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0020037molecular_functionheme binding
A0031408biological_processoxylipin biosynthetic process
A0034614biological_processcellular response to reactive oxygen species
A0042742biological_processdefense response to bacterium
A0046872molecular_functionmetal ion binding
A0050832biological_processdefense response to fungus
A0051213molecular_functiondioxygenase activity
A0071446biological_processcellular response to salicylic acid stimulus
A0071732biological_processcellular response to nitric oxide
A0098869biological_processcellular oxidant detoxification
A1902609biological_process(R)-2-hydroxy-alpha-linolenic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 701
ChainResidue
AALA149
ATHR376
ATYR379
AMET381
AHIS382
AILE416
APHE453
ALEU472
ALEU475
AARG479
AARG483
AILE152
AHOH815
AHOH843
AHOH996
AHOH1180
AGLN153
AVAL156
AHIS157
AASP161
AHIS162
AASN260
ATRP262

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DMU A 702
ChainResidue
ASER19
ALYS20
AMET21
ASER22
APHE23
ALYS26
APHE31
AARG38
AILE348
APG4709
AHOH829
AHOH928
AHOH1055

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PG4 A 703
ChainResidue
AASN54
AARG57

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG A 704
ChainResidue
APHE24

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1PE A 705
ChainResidue
AASN39
AHIS42
ALYS43
AARG492
AILE498
APRO499
AILE500
AASP505
AGLU536
ANA717
AHOH832
AHOH1029
AHOH1117

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE A 706
ChainResidue
AGLU490
AARG493
AARG494
APHE496

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 A 707
ChainResidue
AARG590
ALYS606
ASER608
ATYR618
ANA718

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 708
ChainResidue
AILE239
AGLY240
AASP241
AGLY243
ALYS274

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 A 709
ChainResidue
AALA34
APHE35
AARG38
ADMU702
AHOH1119

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 710
ChainResidue
ALYS323
AARG326
AHOH1023
AHOH1028

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 711
ChainResidue
AARG517
AALA518
AILE519

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 712
ChainResidue
ATHR210
ATRP212
AASP214
ASER216
AHOH874
AHOH1085

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 713
ChainResidue
ALYS309
ATRP333
AHOH1132

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 714
ChainResidue
AARG330
ALYS339
AHOH954

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 715
ChainResidue
AGLY350
AILE352
ALEU353
AHOH922

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 716
ChainResidue
AHIS311
ATYR379

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 717
ChainResidue
AHOH981
AHOH1117
AASP505
A1PE705
AHOH980

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 718
ChainResidue
ASER608
APG4707
AHOH1228

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
AHIS157

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:23934749
ChainResidueDetails
AASP158
AGLU599
AHIS162
ATHR210
ATRP212
AASP214
ASER216
AHIS311
AARG479
AARG483

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:23934749
ChainResidueDetails
AHIS382

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
AARG259

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon