Structure of PDB 1urv Chain B Binding Site BS02

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 IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain1urv Chain B Residue 1172 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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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)		F49 Y59 F60 Q62 H81 R84 H113 H117 V119 Y123 F124 L127
Binding residue
(residue number reindexed from 1)		F32 Y42 F43 Q45 H64 R67 H96 H100 V102 Y106 F107 L110
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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