Structure of PDB 3brx Chain A

Receptor sequence
>3brxA (length=317) Species: 3635 (Gossypium hirsutum) [Search protein sequence]
HHATLTVPTTVPSVSEDCEQLRKAFSGWGTNEGLIIDILGHRNAEQRNLI
RKTYAETYGEDLLKALDKELSNDFERLVLLWALDPAERDALLANEATKRW
TSSNQVLMEIACTRSANQLLHARQAYHARYKKSLEEDVAHHTTGDFHKLL
LPLVSSYRYEGEEVNMTLAKTEAKLLHEKISNKAYSDDDVIRVLATRSKA
QINATLNHYKNEYGNDINKDLKADPKDEFLALLRSTVKCLVYPEKYFEKV
LRLAINRRGTDEGALTRVVCTRAEVDLKVIADEYQRRNSVPLTRAIVKDT
HGDYEKLLLVLAGHVEN
3D structure
PDB3brx The crystal structure of calcium-bound annexin Gh1 from Gossypium hirsutum and its implications for membrane binding mechanisms of plant annexins.
ChainA
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 CA A F29 G31 G33 E73 F25 G27 G29 E69
BS02 CA A I259 R261 G263 D303 I255 R257 G259 D299
BS03 CA A V301 T304 E309 V297 T300 E305
Gene Ontology
Molecular Function
GO:0001786 phosphatidylserine binding
GO:0005509 calcium ion binding
GO:0005544 calcium-dependent phospholipid binding
GO:0046872 metal ion binding
Biological Process
GO:0006950 response to stress
GO:0006979 response to oxidative stress
GO:0009408 response to heat
GO:0009409 response to cold
GO:0009414 response to water deprivation
GO:0009651 response to salt stress
GO:0009835 fruit ripening
GO:0017156 calcium-ion regulated exocytosis
GO:0032940 secretion by cell
GO:0070206 protein trimerization
GO:2001006 regulation of cellulose biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0070382 exocytic vesicle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3brx, PDBe:3brx, PDBj:3brx
PDBsum3brx
PubMed18441010
UniProtP93157|ANX1_GOSHI Annexin Gh1 (Fragment) (Gene Name=AnnGh1)

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