Structure of PDB 2iuk Chain A

Receptor sequence
>2iukA (length=835) Species: 3847 (Glycine max) [Search protein sequence]
GQKIKGTVVLMPKNVLDFNAITSIVIDTATSFLGRNISMQLISATQTDGS
GNGKVGKEVYLEKHLPTLPTLGARQDAFSIFFEWDASFGIPGAFYIKNFM
TDEFFLVSVKLEDIPNHGTIEFVCNSWVYNFRSYKKNRIFFVNDTYLPSA
TPAPLLKYRKEEFEVLRGDGTGKRKDFDRIYDYDVYNDLGNPDGGDPRPI
LGGCSIYPYPLRVRTGRERTRTDPNSEKPGEVYVPRDENFGHLKSSDFLT
YGIKSLSHDVIPLFKSAIFQLRVTSSEFESFEDVRSLYEGGIKLPTDILS
QISPLPALKEIFRTDGENVLQFPPPHVAKVSKSGVMTDEEFAREVIAGVN
PNVIRRLQEFPPKSTLDPTLYGDQTSTITKEQLEINMGGVTVEEALSTQR
LFILDYQDAFIPYLTRINSLPTAKAYATRTILFLKDDGTLKPLAIELSKP
HPDGDNLGPESIVVLPATEGVDSTIWLLAKAHVIVNDSGYHQLVSHWLNT
HAVMEPFAIATNRHLSVLHPIYKLLYPHYRDTININGLARQSLINADGII
EKSFLPGKYSIEMSSSVYKNWVFTHQALPADLVKRGLAIEDPSAPHGLRL
VIEDYPYAVDGLEIWDAIKTWVHEYVSLYYPTDAAVQQDTELQAWWKEAV
EKGHGDLKEKPWWPKKQTTEDLIQSCSIIVWTASALHAAVNFGQYPYGGL
ILNRPTLARRFIPAEGTPEYDEMVKNPQKAYLRTITPKFETLIDLSVIEI
LSRHASDEIYLGERETPNWTTDKKALEAFKRFGSKLTGIEGKINARNSDP
SLRNRTGPVQLPYTLLHRSSEEGLTFKGIPNSISI
3D structure
PDB2iuk Crystal Structures of Vegetative Soybean Lipoxygenase Vlx-B and Vlx-D, and Comparisons with Seed Isoforms Lox-1 and Lox-3.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H525 H530 H716 N720 I864
Catalytic site (residue number reindexed from 1) H496 H501 H687 N691 I835
Enzyme Commision number 1.13.11.58: linoleate 9S-lipoxygenase.
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 FE A H525 H530 H716 N720 I864 H496 H501 H687 N691 I835
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:1990136 linoleate 9S-lipoxygenase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0031408 oxylipin biosynthetic process
GO:0034440 lipid oxidation
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2iuk, PDBe:2iuk, PDBj:2iuk
PDBsum2iuk
PubMed17022084
UniProtP24095|LOXX_SOYBN Seed linoleate 9S-lipoxygenase (Gene Name=LOX1.4)

[Back to BioLiP]