Structure of PDB 1urv Chain B Binding Site BS03

Receptor Information
>1urv Chain B (length=154) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ELSEAERKAVQAMWARLYANSEDVGVAILVRFFVNFPSAKQYFSQFKHME
DPLEMERSPQLRKHASRVMGALNTVVENLHDPDKVSSVLALVGKAHALKH
KVEPVYFKILSGVILEVVAEEFASDFPPETQRAWAKLRGLIYSHVTAAYK
EVGW
Ligand information
Ligand IDFC6
InChIInChI=1S/6CN.Fe/c6*1-2;
InChIKeyHCMVSLMENOCDCK-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(#N)[Fe](C#N)(C#N)(C#N)(C#N)C#N
ACDLabs 10.04
CACTVS 3.341		N#C[Fe](C#N)(C#N)(C#N)(C#N)C#N
FormulaC6 Fe N6
NameHEXACYANOFERRATE(3-);
FERRI(III)HEXACYANIDE
ChEMBL
DrugBank
ZINC
PDB chain1urv Chain B Residue 1173 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1urv Crystal Structure of Cytoglobin: The Fourth Globin Type Discovered in Man Displays Heme Hexa-Coordination.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		K125 R155 G156 Y159
Binding residue
(residue number reindexed from 1)		K108 R138 G139 Y142
Annotation score1
Enzymatic activity
Enzyme Commision number 1.11.1.-
1.14.12.-
1.15.1.1: superoxide dismutase.
1.7.-.-
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:1urv, PDBe:1urv, PDBj:1urv
PDBsum1urv
PubMed15095869
UniProtQ8WWM9|CYGB_HUMAN Cytoglobin (Gene Name=CYGB)

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