eF-site ID 1ed4-AB PDB Code 1ed4 Chain A, B click to enlarge Title BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH IPITU (H4B FREE) Classification OXIDOREDUCTASE Compound NITRIC OXIDE SYNTHASE Source Bos taurus (Bovine) (NOS3_BOVIN) Sequence A:  GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLV LPRKLQTRPSPGPPPAEQLLSQARDFINQYYSSIKRSGSQ AHEERLQEVEAEVASTGTYHLRESELVFGAKQAWRNAPRC VGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNL RSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGD PANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFV LPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIG GLEFSAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMD LDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAAT VSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEM VNYILSPAFRYQPDPW B:  KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLP RKLQTRPSPGPPPAEQLLSQARDFINQYYSSIKRSGSQAH EERLQEVEAEVASTGTYHLRESELVFGAKQAWRNAPRCVG RIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRS AITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPA NVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLP PELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGL EFSAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLD TRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVS FMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVN YILSPAFRYQPDPW Description Functional site 1) chain A residue 249 type sequence Q description BINDING SITE FOR RESIDUE ACT A 1850 source : AC1 2) chain A residue 252 type sequence R description BINDING SITE FOR RESIDUE ACT A 1850 source : AC1 3) chain A residue 368 type sequence N description BINDING SITE FOR RESIDUE ACT A 1850 source : AC1 4) chain A residue 374 type sequence R description BINDING SITE FOR RESIDUE ACT A 1850 source : AC1 5) chain A residue 358 type sequence W description BINDING SITE FOR RESIDUE ACT A 1860 source : AC2 6) chain A residue 420 type sequence V description BINDING SITE FOR RESIDUE ACT A 1860 source : AC2 7) chain A residue 428 type sequence S description BINDING SITE FOR RESIDUE ACT A 1860 source : AC2 8) chain B residue 252 type sequence R description BINDING SITE FOR RESIDUE ACT B 2850 source : AC3 9) chain B residue 368 type sequence N description BINDING SITE FOR RESIDUE ACT B 2850 source : AC3 10) chain B residue 374 type sequence R description BINDING SITE FOR RESIDUE ACT B 2850 source : AC3 11) chain B residue 188 type sequence G description BINDING SITE FOR RESIDUE ACT B 2860 source : AC4 12) chain B residue 358 type sequence W description BINDING SITE FOR RESIDUE ACT B 2860 source : AC4 13) chain B residue 420 type sequence V description BINDING SITE FOR RESIDUE ACT B 2860 source : AC4 14) chain B residue 428 type sequence S description BINDING SITE FOR RESIDUE ACT B 2860 source : AC4 15) chain A residue 96 type sequence C description BINDING SITE FOR RESIDUE ZN A 900 source : AC5 16) chain A residue 101 type sequence C description BINDING SITE FOR RESIDUE ZN A 900 source : AC5 17) chain B residue 96 type sequence C description BINDING SITE FOR RESIDUE ZN A 900 source : AC5 18) chain B residue 101 type sequence C description BINDING SITE FOR RESIDUE ZN A 900 source : AC5 19) chain A residue 180 type sequence W description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 20) chain A residue 185 type sequence R description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 21) chain A residue 186 type sequence C description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 22) chain A residue 228 type sequence S description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 23) chain A residue 355 type sequence F description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 24) chain A residue 356 type sequence S description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 25) chain A residue 358 type sequence W description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 26) chain A residue 363 type sequence E description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 27) chain A residue 449 type sequence W description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 28) chain A residue 477 type sequence Y description BINDING SITE FOR RESIDUE HEM A 1500 source : AC6 29) chain A residue 336 type sequence P description BINDING SITE FOR RESIDUE IPU A 1830 source : AC7 30) chain A residue 338 type sequence V description BINDING SITE FOR RESIDUE IPU A 1830 source : AC7 31) chain A residue 355 type sequence F description BINDING SITE FOR RESIDUE IPU A 1830 source : AC7 32) chain A residue 356 type sequence S description BINDING SITE FOR RESIDUE IPU A 1830 source : AC7 33) chain A residue 358 type sequence W description BINDING SITE FOR RESIDUE IPU A 1830 source : AC7 34) chain A residue 363 type sequence E description BINDING SITE FOR RESIDUE IPU A 1830 source : AC7 35) chain A residue 106 type sequence V description BINDING SITE FOR RESIDUE IPU B 1840 source : AC8 36) chain A residue 448 type sequence A description BINDING SITE FOR RESIDUE IPU B 1840 source : AC8 37) chain A residue 449 type sequence W description BINDING SITE FOR RESIDUE IPU B 1840 source : AC8 38) chain B residue 447 type sequence W description BINDING SITE FOR RESIDUE IPU B 1840 source : AC8 39) chain B residue 462 type sequence F description BINDING SITE FOR RESIDUE IPU B 1840 source : AC8 40) chain B residue 463 type sequence H description BINDING SITE FOR RESIDUE IPU B 1840 source : AC8 41) chain A residue 324 type sequence W description BINDING SITE FOR RESIDUE CAD A 1950 source : AC9 42) chain A residue 384 type sequence C description BINDING SITE FOR RESIDUE CAD A 1950 source : AC9 43) chain B residue 180 type sequence W description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 44) chain B residue 185 type sequence R description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 45) chain B residue 186 type sequence C description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 46) chain B residue 228 type sequence S description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 47) chain B residue 355 type sequence F description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 48) chain B residue 356 type sequence S description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 49) chain B residue 358 type sequence W description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 50) chain B residue 363 type sequence E description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 51) chain B residue 449 type sequence W description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 52) chain B residue 477 type sequence Y description BINDING SITE FOR RESIDUE HEM B 2500 source : BC1 53) chain B residue 336 type sequence P description BINDING SITE FOR RESIDUE IPU B 2830 source : BC2 54) chain B residue 355 type sequence F description BINDING SITE FOR RESIDUE IPU B 2830 source : BC2 55) chain B residue 356 type sequence S description BINDING SITE FOR RESIDUE IPU B 2830 source : BC2 56) chain B residue 358 type sequence W description BINDING SITE FOR RESIDUE IPU B 2830 source : BC2 57) chain B residue 359 type sequence Y description BINDING SITE FOR RESIDUE IPU B 2830 source : BC2 58) chain B residue 363 type sequence E description BINDING SITE FOR RESIDUE IPU B 2830 source : BC2 59) chain A residue 447 type sequence W description BINDING SITE FOR RESIDUE IPU A 2840 source : BC3 60) chain A residue 462 type sequence F description BINDING SITE FOR RESIDUE IPU A 2840 source : BC3 61) chain A residue 463 type sequence H description BINDING SITE FOR RESIDUE IPU A 2840 source : BC3 62) chain B residue 104 type sequence S description BINDING SITE FOR RESIDUE IPU A 2840 source : BC3 63) chain B residue 448 type sequence A description BINDING SITE FOR RESIDUE IPU A 2840 source : BC3 64) chain B residue 449 type sequence W description BINDING SITE FOR RESIDUE IPU A 2840 source : BC3 65) chain B residue 83 type sequence Y description BINDING SITE FOR RESIDUE CAD B 2950 source : BC4 66) chain B residue 324 type sequence W description BINDING SITE FOR RESIDUE CAD B 2950 source : BC4 67) chain B residue 384 type sequence C description BINDING SITE FOR RESIDUE CAD B 2950 source : BC4 68) chain A residue 367 type sequence R description BINDING SITE FOR RESIDUE GOL B 1880 source : BC5 69) chain A residue 448 type sequence A description BINDING SITE FOR RESIDUE GOL B 1880 source : BC5 70) chain A residue 449 type sequence W description BINDING SITE FOR RESIDUE GOL B 1880 source : BC5 71) chain B residue 462 type sequence F description BINDING SITE FOR RESIDUE GOL B 1880 source : BC5 72) chain A residue 263 type sequence V description BINDING SITE FOR RESIDUE GOL A 1885 source : BC6 73) chain A residue 265 type sequence G description BINDING SITE FOR RESIDUE GOL A 1885 source : BC6 74) chain A residue 267 type sequence P description BINDING SITE FOR RESIDUE GOL A 1885 source : BC6 75) chain A residue 287 type sequence R description BINDING SITE FOR RESIDUE GOL A 1885 source : BC6 76) chain A residue 375 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1885 source : BC6 77) chain A residue 462 type sequence F description BINDING SITE FOR RESIDUE GOL A 2880 source : BC7 78) chain A residue 463 type sequence H description BINDING SITE FOR RESIDUE GOL A 2880 source : BC7 79) chain B residue 104 type sequence S description BINDING SITE FOR RESIDUE GOL A 2880 source : BC7 80) chain B residue 106 type sequence V description BINDING SITE FOR RESIDUE GOL A 2880 source : BC7 81) chain B residue 449 type sequence W description BINDING SITE FOR RESIDUE GOL A 2880 source : BC7 82) chain B residue 263 type sequence V description BINDING SITE FOR RESIDUE GOL B 2885 source : BC8 83) chain B residue 265 type sequence G description BINDING SITE FOR RESIDUE GOL B 2885 source : BC8 84) chain B residue 267 type sequence P description BINDING SITE FOR RESIDUE GOL B 2885 source : BC8 85) chain B residue 287 type sequence R description BINDING SITE FOR RESIDUE GOL B 2885 source : BC8 86) chain B residue 374 type sequence R description BINDING SITE FOR RESIDUE GOL B 2885 source : BC8 87) chain B residue 375 type sequence Y description BINDING SITE FOR RESIDUE GOL B 2885 source : BC8 88) chain A residue 142 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 89) chain B residue 397 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 90) chain B residue 401 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 91) chain B residue 406 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 92) chain A residue 287 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 93) chain A residue 396 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 94) chain A residue 397 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 95) chain A residue 401 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 96) chain A residue 406 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 97) chain B residue 142 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 98) chain B residue 287 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 99) chain B residue 396 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 100) chain A residue 224 type BINDING sequence G description axial binding residue => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI3 101) chain B residue 224 type BINDING sequence G description axial binding residue => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI3 102) chain A residue 154 type MOD_RES sequence E description Phosphoserine; by CDK5 => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI4 103) chain B residue 154 type MOD_RES sequence E description Phosphoserine; by CDK5 => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI4 104) chain A residue 134 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P35228 source Swiss-Prot : SWS_FT_FI1 105) chain A residue 139 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P35228 source Swiss-Prot : SWS_FT_FI1 106) chain B residue 134 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P35228 source Swiss-Prot : SWS_FT_FI1 107) chain B residue 139 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P35228 source Swiss-Prot : SWS_FT_FI1 108) chain A residue 185-192 type prosite sequence RCVGRIQW description NOS Nitric oxide synthase (NOS) signature. RCVGRIqW source prosite : PS60001

Display surface Download Links