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1NO3

REFINED STRUCTURE OF SOYBEAN LIPOXYGENASE-3 WITH 4-NITROCATECHOL AT 2.15 ANGSTROM RESOLUTION

Replaces:  1BYT
Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0031408biological_processoxylipin biosynthetic process
A0034440biological_processlipid oxidation
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A1990136molecular_functionlinoleate 9S-lipoxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 858
ChainResidue
AHIS518
AHIS523
AHIS709
AASN713
AILE857
AHOH1533

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 4NC A 859
ChainResidue
AHIS523
AILE557
ALEU565
AILE572
ALEU773
AILE857
AGLN514
AHIS518
ATRP519

Functional Information from PROSITE/UniProt
site_idPS00081
Number of Residues11
DetailsLIPOXYGENASE_2 Lipoxygenases iron-binding region signature 2. VHPIyKLLhPH
ChainResidueDetails
AVAL540-HIS550

site_idPS00711
Number of Residues15
DetailsLIPOXYGENASE_1 Lipoxygenases iron-binding region signature 1. HQlvsHwLNTHAVvE
ChainResidueDetails
AHIS513-GLU527

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues125
DetailsDomain: {"description":"PLAT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00152","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues691
DetailsDomain: {"description":"Lipoxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00726","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues45
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsCompositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues13
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lnh
ChainResidueDetails
AASN713

site_idMCSA1
Number of Residues5
DetailsM-CSA 583
ChainResidueDetails
AHIS518
AHIS523
AHIS709
AASN713electrostatic stabiliser
AILE857

238582

PDB entries from 2025-07-09

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