Structure of PDB 2jlp Chain B

Receptor sequence
>2jlpB (length=166) Species: 9606 (Homo sapiens) [Search protein sequence]
GTLHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEP
NSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSL
WRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLA
CCVVGVCGPGLWERQA
3D structure
PDB2jlp The Structure of Human Extracellular Copper-Zinc Superoxide Dismutase at 1.7 A Resolution: Insights Into Heparin and Collagen Binding.
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H96 H98 H113 H121 H124 D127 H163 R186
Catalytic site (residue number reindexed from 1) H58 H60 H75 H83 H86 D89 H125 R148
Enzyme Commision number 1.15.1.1: superoxide dismutase.
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 CU B H96 H98 H163 H58 H60 H125
BS02 ZN B H113 H121 H124 D127 H75 H83 H86 D89
Gene Ontology
Molecular Function
GO:0004784 superoxide dismutase activity
GO:0005507 copper ion binding
GO:0005515 protein binding
GO:0008201 heparin binding
GO:0016209 antioxidant activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0060090 molecular adaptor activity
Biological Process
GO:0001666 response to hypoxia
GO:0006801 superoxide metabolic process
GO:0006979 response to oxidative stress
GO:0019430 removal of superoxide radicals
GO:0046688 response to copper ion
GO:0097746 blood vessel diameter maintenance
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005794 Golgi apparatus
GO:0005796 Golgi lumen
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2jlp, PDBe:2jlp, PDBj:2jlp
PDBsum2jlp
PubMed19289127
UniProtP08294|SODE_HUMAN Extracellular superoxide dismutase [Cu-Zn] (Gene Name=SOD3)

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