about
P361
Cytochrome P450 family 27 subfamily B member 1Cytochrome P450 family 1 subfamily A member 1Hemoglobin subunit alpha 2Cytochrome P450, family 21, subfamily a, polypeptide 1Cytochrome P450, family 27, subfamily b, polypeptide 1MyoglobinCatalaseCytochrome P450, family 2, subfamily d, polypeptide 10Cytochrome P450, family 2, subfamily e, polypeptide 1MyeloperoxidaseSuccinate dehydrogenase complex, subunit D, integral membrane proteinSuccinate dehydrogenase complex, subunit C, integral membrane proteinCytochrome P450, family 19, subfamily a, polypeptide 1Cytochrome b-245, beta polypeptideHemopexinThromboxane A synthase 1, plateletHeme oxygenase 1Cytochrome P450, family 1, subfamily a, polypeptide 2Cytochrome P450, family 1, subfamily b, polypeptide 1Cytochrome P450, family 17, subfamily a, polypeptide 1Cytochrome P450, family 11, subfamily a, polypeptide 1Cytochrome P450, family 27, subfamily a, polypeptide 1Eosinophil peroxidaseCytochrome P450, family 7, subfamily a, polypeptide 1Indoleamine 2,3-dioxygenase 1Cytochrome P450, family 11, subfamily b, polypeptide 2Prostaglandin I2 (prostacyclin) synthaseCystathionine beta-synthaseJanus kinase 2Cytochrome P450, family 2, subfamily c, polypeptide 55Cytochrome P450, family 2, subfamily c, polypeptide 29Sulfite oxidaseCytochrome P450, family 1, subfamily a, polypeptide 1Cytochrome P450 family 27 subfamily A member 1Nuclear receptor subfamily 1 group D member 1Nuclear receptor subfamily 1, group D, member 1Nitric oxide synthase 3, endothelial cellMyoglobinCytochrome c oxidase assembly homolog COX15Cytochrome P450 family 7 subfamily B member 1
P680
Structure of tetragonal crystals of human erythrocyte catalaseStructural basis of drug binding to CYP46A1, an enzyme that controls cholesterol turnover in the brainCrystal structure of a cytochrome P450 2B6 genetic variant in complex with the inhibitor 4-(4-chlorophenyl)imidazole at 2.0-A resolutionAdaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2Crystal structure of human cytochrome P450 2D6The Fowler syndrome-associated protein FLVCR2 is an importer of hemeStructural basis of human CYP51 inhibition by antifungal azolesThe BTB and CNC homology 1 (BACH1) target genes are involved in the oxidative stress response and in control of the cell cycleStructural characterization of human cytochrome P450 2C19: active site differences between P450s 2C8, 2C9, and 2C19Structure of the human lung cytochrome P450 2A13Identification of a mammalian mitochondrial porphyrin transporterHeme controls the regulation of protein tyrosine kinases Jak2 and SrcCrystal structure of the human prostacyclin synthaseStructures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalenStructural characterization of the complex between alpha-naphthoflavone and human cytochrome P450 1B1Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substratescDNA cloning of human retinoic acid-metabolizing enzyme (hP450RAI) identifies a novel family of cytochromes P450Cytochrome c in the apoptotic and antioxidant cascadesStructures of Prostacyclin Synthase and Its Complexes with Substrate Analog and Inhibitor Reveal a Ligand-specific Heme Conformation ChangeBinding of a Cyano- and Fluoro-containing Drug Bicalutamide to Cytochrome P450 46A1: UNUSUAL FEATURES AND SPECTRAL RESPONSEAnalysis of Oligomerization Properties of Heme a Synthase Provides Insights into Its Function in Eukaryotes.Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteinsHuman Cytochrome P450 21A2, the Major Steroid 21-Hydroxylase: STRUCTURE OF THE ENZYME·PROGESTERONE SUBSTRATE COMPLEX AND RATE-LIMITING C-H BOND CLEAVAGEIdentification of thromboxane synthase amino acid residues involved in heme-propionate bindingFunctional expression and characterization of human 101F6 protein, a homologue of cytochrome b561 and a candidate tumor suppressor gene product.The molecular basis of transient heme-protein interactions: analysis, concept and implementation
P921
Q1149122-69A2D591-D5C8-486C-916A-DB47B5C26A5FQ1407929-28EA8011-38A9-4136-A017-3AB468CC0E6BQ1417916-6227AE0F-F97C-4A8A-B8A1-1DA0AECB7AACQ1417916-E254BF6D-6E9B-43B8-AF80-522FFA9859AEQ14358870-23A3CDFD-0FB9-49D5-99DE-2F54D6667682Q14599791-17AC26FB-6BF9-46C9-88E3-7683A7E033E3Q14819304-54C0B9EB-67F1-4CA9-A58A-0DD87DAF404CQ14849204-BBFCC6DE-9A01-4680-A854-A1E395FA8064Q14864429-7A43DE32-5E47-44EB-80EA-A12FD2ECAD85Q14864429-F3B90663-8F2B-4916-AF18-D87E57EB939CQ14864436-6A751F83-5DBE-463F-BD4B-CAF06A354297Q14864436-E1884AAC-6518-419B-8C03-17DC1071B7E1Q14864838-A03D5C3E-E61A-47F7-9E39-D630C9B2869EQ14864966-0EFD6263-9810-49D8-912E-31BCEE11650FQ14864973-08D31906-FB47-4FBC-A036-01A3B3676452Q14864973-94CF0D23-BA02-4FD6-9749-1B4DBD043D2BQ14865019-11F3E3DC-0C90-482C-B454-9460486ED0B7Q14875845-24E2DF6F-792C-48AB-97BA-DA8344BD6707Q14876682-E3079EC1-3F6F-40DB-A7FD-5CA32B93A3FAQ14881698-96BF252C-D7D8-4111-A599-4286E2B6B264Q14882925-DB8DCEB3-FD11-4EDA-9D9A-9490F48FCF9BQ14890105-C0CC8CC2-5595-4C72-8025-51B04AA83DFCQ14905167-22DB7962-4C91-4C04-A797-392CD960E44DQ14905209-EAC53181-9FED-4BEE-9B35-2507124FB1A9Q14905668-578EB290-89D9-4944-A064-62D9E089978CQ14905956-43F0BC1B-2D12-4620-B00E-75F5813D7281Q14905956-98E9AD45-1DEE-4858-9DEE-F478E4DD592FQ14905956-B56094E1-6E25-4011-B476-8BF915DEB063Q14906789-7ABBE5A6-8802-4D80-9893-DA2DA60AA607Q14907377-3FCC9BFF-61F0-4389-BA39-826515D9711DQ14907419-F9F3C4D4-E8E2-47C5-BF3F-CB27588057C0Q14907857-19D17E9A-3BDA-4A0C-865D-45E81377A701Q14911843-138B2327-D3AF-4D4E-82E6-260E0669158FQ14911843-51D4F823-44D2-4328-A342-08AB377B6318Q14913099-6C258BAE-2537-452E-953F-850516C52EECQ14914518-DB963AC7-7136-47FB-AF74-F272521BEBA6Q14916185-533FEB59-61FB-4D8C-8D74-F014A5AFC239Q14916185-5C12FB8C-169A-44E8-B480-A27EFE03CDFBQ14916192-92B24724-8C52-4F85-8D83-2D5A7AF3805CQ14916192-D034B2C6-94EC-4C1D-92B8-25CE41A794D6
P680
Q24290679-8EF4D4D0-F432-482E-8A34-21C81F569CC9Q24293342-BD0176A7-420F-42C8-9F70-108B3CD1F152Q24294558-26DC5980-FE68-4572-8515-504ACF240310Q24297785-FF7194E9-E559-4AEC-9F9D-7D59DE8142D8Q24298673-018993AB-B5D6-44BD-8C9F-D3ECA9AD09D6Q24298998-921214E4-B801-417A-BA42-AE32ADC54AC4Q24299075-C5EC0FB1-2D4A-4F29-B503-8ADF3DCBAFA7Q24301823-5A96B002-33BA-4F7E-A87C-DDAC396676E3Q24302187-3763C2A4-B1F7-4313-9E7A-CF4C3A1EAEDAQ24302407-92A5E863-192C-4CCB-8C33-1891BE5122D9Q24305008-D3DE0C7B-E8BD-49AE-81E9-27FD9D1F05F7Q24305018-F245162F-2071-4AC3-AC89-EE2E8B1D8CA2Q24305553-6A057B68-9A96-48C0-8A77-6AE59C585B3CQ24313478-FD130F4A-146F-43E1-9C6E-24026E4E35C7Q24314798-9C8077FE-2D06-4595-8384-7DE00A9D9F86Q24316102-A1155D47-70B1-49A6-ACEC-FA6C67191F65Q24318445-BF40995E-D08E-438E-B7FD-A5DFCCE6D7CAQ24318915-23F2AD51-E938-4EA5-9BAB-B3D9DF7ABF76Q27649121-0CD097ED-E9B4-4B5F-B7CF-4670C08F061EQ27675738-62334FF6-F66C-4232-ADAB-8D8F81919DBFQ27931313-49842DC5-228F-4507-8AD4-A3F5177ADBC1Q28115078-16EEC41D-3CCE-4CC2-B932-855A707B1A85Q28117252-6D9BA506-3C7C-4ECE-828E-9A50B46453D2Q28138838-3598CD12-7CF7-41CD-BE2C-E1E87F331997Q33500523-34BFB3ED-D577-4B62-88F2-64C92EECA996Q61805821-5090D1B2-B3A1-4C92-89D1-A52FAAAE938B
P921
description
Heme bindend
@nl
Interacting selectively and no ...... porphyrin (tetrapyrrole) ring.
@en
name
Heme binding
@nl
Häm-bindend
@de
heme bindin
@sco
heme binding
@en
hæm binding
@da
type
label
Heme binding
@nl
Häm-bindend
@de
heme bindin
@sco
heme binding
@en
hæm binding
@da
altLabel
GO:0020037
@en
Häm-bindende
@de
Häm-bindender
@de
Häm-bindendes
@de
haem binding
@en
hæm-bindende
@da
prefLabel
Heme binding
@nl
Häm-bindend
@de
heme bindin
@sco
heme binding
@en
hæm binding
@da
P2888
P527
P686
GO:0020037