eF-site ID 1dm6-AB PDB Code 1dm6 Chain A, B click to enlarge Title BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH N-(4-CHLOROPHENYL)-N'-HYDROXYGUANIDINE (H4B FREE) Classification OXIDOREDUCTASE Compound NITRIC OXIDE SYNTHASE Source null (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 252 type sequence R description BINDING SITE FOR RESIDUE ACT A 1850 source : AC1 2) chain A residue 368 type sequence N description BINDING SITE FOR RESIDUE ACT A 1850 source : AC1 3) chain A residue 374 type sequence R description BINDING SITE FOR RESIDUE ACT A 1850 source : AC1 4) chain A residue 188 type sequence G description BINDING SITE FOR RESIDUE ACT A 1860 source : AC2 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 A residue 324 type sequence W description BINDING SITE FOR RESIDUE CAC A 950 source : AC3 9) chain A residue 384 type sequence C description BINDING SITE FOR RESIDUE CAC A 950 source : AC3 10) chain A residue 438 type sequence K description BINDING SITE FOR RESIDUE CAC A 950 source : AC3 11) chain A residue 441 type sequence G description BINDING SITE FOR RESIDUE CAC A 950 source : AC3 12) chain B residue 249 type sequence Q description BINDING SITE FOR RESIDUE ACT B 2850 source : AC4 13) chain B residue 252 type sequence R description BINDING SITE FOR RESIDUE ACT B 2850 source : AC4 14) chain B residue 368 type sequence N description BINDING SITE FOR RESIDUE ACT B 2850 source : AC4 15) chain B residue 374 type sequence R description BINDING SITE FOR RESIDUE ACT B 2850 source : AC4 16) chain B residue 188 type sequence G description BINDING SITE FOR RESIDUE ACT B 2860 source : AC5 17) chain B residue 358 type sequence W description BINDING SITE FOR RESIDUE ACT B 2860 source : AC5 18) chain B residue 420 type sequence V description BINDING SITE FOR RESIDUE ACT B 2860 source : AC5 19) chain B residue 428 type sequence S description BINDING SITE FOR RESIDUE ACT B 2860 source : AC5 20) chain B residue 83 type sequence Y description BINDING SITE FOR RESIDUE CAC B 950 source : AC6 21) chain B residue 324 type sequence W description BINDING SITE FOR RESIDUE CAC B 950 source : AC6 22) chain B residue 384 type sequence C description BINDING SITE FOR RESIDUE CAC B 950 source : AC6 23) chain A residue 96 type sequence C description BINDING SITE FOR RESIDUE ZN A 900 source : AC7 24) chain A residue 101 type sequence C description BINDING SITE FOR RESIDUE ZN A 900 source : AC7 25) chain B residue 96 type sequence C description BINDING SITE FOR RESIDUE ZN A 900 source : AC7 26) chain B residue 101 type sequence C description BINDING SITE FOR RESIDUE ZN A 900 source : AC7 27) chain A residue 180 type sequence W description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 28) chain A residue 185 type sequence R description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 29) chain A residue 186 type sequence C description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 30) chain A residue 355 type sequence F description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 31) chain A residue 356 type sequence S description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 32) chain A residue 358 type sequence W description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 33) chain A residue 449 type sequence W description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 34) chain A residue 475 type sequence F description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 35) chain A residue 477 type sequence Y description BINDING SITE FOR RESIDUE HEM A 1500 source : AC8 36) chain A residue 338 type sequence V description BINDING SITE FOR RESIDUE PH3 A 1780 source : AC9 37) chain A residue 357 type sequence G description BINDING SITE FOR RESIDUE PH3 A 1780 source : AC9 38) chain A residue 358 type sequence W description BINDING SITE FOR RESIDUE PH3 A 1780 source : AC9 39) chain A residue 363 type sequence E description BINDING SITE FOR RESIDUE PH3 A 1780 source : AC9 40) chain A residue 104 type sequence S description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 41) chain A residue 367 type sequence R description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 42) chain A residue 448 type sequence A description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 43) chain A residue 449 type sequence W description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 44) chain B residue 447 type sequence W description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 45) chain B residue 462 type sequence F description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 46) chain B residue 463 type sequence H description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 47) chain B residue 464 type sequence Q description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 48) chain B residue 465 type sequence E description BINDING SITE FOR RESIDUE PH3 B 1785 source : BC1 49) chain B residue 180 type sequence W description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 50) chain B residue 185 type sequence R description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 51) chain B residue 186 type sequence C description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 52) chain B residue 228 type sequence S description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 53) chain B residue 355 type sequence F description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 54) chain B residue 356 type sequence S description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 55) chain B residue 358 type sequence W description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 56) chain B residue 363 type sequence E description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 57) chain B residue 449 type sequence W description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 58) chain B residue 475 type sequence F description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 59) chain B residue 477 type sequence Y description BINDING SITE FOR RESIDUE HEM B 2500 source : BC2 60) chain A residue 447 type sequence W description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 61) chain A residue 462 type sequence F description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 62) chain A residue 463 type sequence H description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 63) chain A residue 464 type sequence Q description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 64) chain A residue 465 type sequence E description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 65) chain B residue 104 type sequence S description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 66) chain B residue 367 type sequence R description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 67) chain B residue 448 type sequence A description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 68) chain B residue 449 type sequence W description BINDING SITE FOR RESIDUE PH3 A 2785 source : BC3 69) chain B residue 338 type sequence V description BINDING SITE FOR RESIDUE PH3 B 2780 source : BC4 70) chain B residue 357 type sequence G description BINDING SITE FOR RESIDUE PH3 B 2780 source : BC4 71) chain B residue 358 type sequence W description BINDING SITE FOR RESIDUE PH3 B 2780 source : BC4 72) chain B residue 363 type sequence E description BINDING SITE FOR RESIDUE PH3 B 2780 source : BC4 73) chain A residue 186 type BINDING sequence C description axial binding residue => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI3 74) chain B residue 186 type BINDING sequence C description axial binding residue => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 96 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P35228 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 101 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P35228 source Swiss-Prot : SWS_FT_FI1 77) chain A residue 96 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P35228 source Swiss-Prot : SWS_FT_FI1 78) chain A residue 101 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P35228 source Swiss-Prot : SWS_FT_FI1 79) chain A residue 185-192 type prosite sequence RCVGRIQW description NOS Nitric oxide synthase (NOS) signature. RCVGRIqW source prosite : PS60001 80) chain A residue 116 type MOD_RES sequence S description Phosphoserine; by CDK5 => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI4 81) chain B residue 116 type MOD_RES sequence S description Phosphoserine; by CDK5 => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI4 82) chain A residue 249 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 83) chain A residue 477 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 84) chain B residue 104 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 85) chain B residue 249 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 86) chain B residue 358 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 87) chain B residue 359 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 88) chain B residue 363 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 89) chain B residue 368 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 90) chain B residue 448 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 91) chain B residue 449 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 92) chain B residue 462 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 93) chain B residue 477 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 94) chain A residue 358 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 95) chain A residue 359 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 96) chain A residue 363 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 97) chain A residue 368 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 98) chain A residue 448 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 99) chain A residue 449 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 100) chain A residue 462 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2 101) chain A residue 104 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI2

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