Structure of PDB 1ury Chain A

Receptor sequence
>1uryA (length=154) Species: 9606 (Homo sapiens) [Search protein sequence]
ELSEAERKAVQAMWARLYANSEDVGVAILVRFFVNFPSAKQYFSQFKHME
DPLEMERSPQLRKHASRVMGALNTVVENLHDPDKVSSVLALVGKAHALKH
KVEPVYFKILSGVILEVVAEEFASDFPPETQRAWAKLRGLIYSHVTAAYK
EVGW
3D structure
PDB1ury Cytoglobin Cavities
ChainA
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.1.-
1.14.12.-
1.15.1.1: superoxide dismutase.
1.7.-.-
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 HEM A Y59 F60 Q77 H81 R84 V109 H113 H117 V119 Y123 F124 Y42 F43 Q60 H64 R67 V92 H96 H100 V102 Y106 F107
BS02 XE A G42 I45 V85 M86 G25 I28 V68 M69
BS03 XE A W31 M86 W14 M69
BS04 FC6 A K125 R155 Y159 K108 R138 Y142
BS05 XE A I131 R155 I114 R138
BS06 FC6 A F53 P54 S55 F36 P37 S38
Gene Ontology
Molecular Function
GO:0004096 catalase activity
GO:0004601 peroxidase activity
GO:0004784 superoxide dismutase activity
GO:0005344 oxygen carrier activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0047888 fatty acid peroxidase activity
GO:0070025 carbon monoxide binding
GO:0098809 nitrite reductase activity
GO:0141118 nitric oxide dioxygenase activity, heme protein as donor
Biological Process
GO:0001666 response to hypoxia
GO:0006979 response to oxidative stress
GO:0010764 negative regulation of fibroblast migration
GO:0015671 oxygen transport
GO:0019395 fatty acid oxidation
GO:0019430 removal of superoxide radicals
GO:0032966 negative regulation of collagen biosynthetic process
GO:0046210 nitric oxide catabolic process
GO:2000490 negative regulation of hepatic stellate cell activation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0043005 neuron projection
GO:0043025 neuronal cell body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ury, PDBe:1ury, PDBj:1ury
PDBsum1ury
PubMed15044115
UniProtQ8WWM9|CYGB_HUMAN Cytoglobin (Gene Name=CYGB)

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