eF-site ID 6av6-C PDB Code 6av6 Chain C click to enlarge Title Structure of human endothelial nitric oxide synthase heme domain in complex with 6-(3-Fluoro-5-(3-(methylamino)propyl)phenethyl)-4-methylpyridin-2-amine Classification OXIDOREDUCTASE Compound Nitric oxide synthase, endothelial Source (NOS3_HUMAN) Sequence C:  FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPA PEQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAA TGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDAR DCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRG DFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGW TPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPT LEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMS TEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAA VEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARG GCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDP W Description Functional site 1) chain C residue 261 type sequence V description binding site for residue BTB B 505 source : AD4 2) chain C residue 373 type sequence Y description binding site for residue BTB B 505 source : AD4 3) chain C residue 374 type sequence N description binding site for residue BTB B 505 source : AD4 4) chain C residue 378 type sequence D description binding site for residue BTB B 505 source : AD4 5) chain C residue 381 type sequence V description binding site for residue BTB B 509 source : AD8 6) chain C residue 382 type sequence C description binding site for residue BTB B 509 source : AD8 7) chain C residue 384 type sequence D description binding site for residue BTB B 509 source : AD8 8) chain C residue 377 type sequence E description binding site for residue BTB B 510 source : AD9 9) chain C residue 178 type sequence W description binding site for residue HEM C 501 source : AE1 10) chain C residue 184 type sequence C description binding site for residue HEM C 501 source : AE1 11) chain C residue 226 type sequence S description binding site for residue HEM C 501 source : AE1 12) chain C residue 353 type sequence F description binding site for residue HEM C 501 source : AE1 13) chain C residue 354 type sequence S description binding site for residue HEM C 501 source : AE1 14) chain C residue 355 type sequence G description binding site for residue HEM C 501 source : AE1 15) chain C residue 356 type sequence W description binding site for residue HEM C 501 source : AE1 16) chain C residue 361 type sequence E description binding site for residue HEM C 501 source : AE1 17) chain C residue 447 type sequence W description binding site for residue HEM C 501 source : AE1 18) chain C residue 473 type sequence F description binding site for residue HEM C 501 source : AE1 19) chain C residue 475 type sequence Y description binding site for residue HEM C 501 source : AE1 20) chain C residue 102 type sequence S description binding site for residue H4B C 502 source : AE2 21) chain C residue 365 type sequence R description binding site for residue H4B C 502 source : AE2 22) chain C residue 446 type sequence A description binding site for residue H4B C 502 source : AE2 23) chain C residue 447 type sequence W description binding site for residue H4B C 502 source : AE2 24) chain C residue 105 type sequence F description binding site for residue W68 C 503 source : AE3 25) chain C residue 336 type sequence V description binding site for residue W68 C 503 source : AE3 26) chain C residue 353 type sequence F description binding site for residue W68 C 503 source : AE3 27) chain C residue 356 type sequence W description binding site for residue W68 C 503 source : AE3 28) chain C residue 361 type sequence E description binding site for residue W68 C 503 source : AE3 29) chain C residue 447 type sequence W description binding site for residue W68 C 503 source : AE3 30) chain C residue 298 type sequence E description binding site for residue BTB C 504 source : AE4 31) chain C residue 94 type sequence C description binding site for residue ZN C 505 source : AE5 32) chain C residue 99 type sequence C description binding site for residue ZN C 505 source : AE5 33) chain C residue 167 type sequence E description binding site for residue GOL C 506 source : AE6 34) chain C residue 247 type sequence Q description binding site for residue CL C 507 source : AE7 35) chain C residue 357 type sequence Y description binding site for residue CL C 507 source : AE7 36) chain C residue 366 type sequence N description binding site for residue CL C 507 source : AE7 37) chain C residue 445 type sequence W description binding site for residue H4B D 502 source : AF1 38) chain C residue 460 type sequence F description binding site for residue H4B D 502 source : AF1 39) chain C residue 461 type sequence H description binding site for residue H4B D 502 source : AF1 40) chain C residue 462 type sequence Q description binding site for residue H4B D 502 source : AF1 41) chain C residue 463 type sequence E description binding site for residue H4B D 502 source : AF1 42) chain C residue 184 type catalytic sequence C description 935 source MCSA : MCSA3 43) chain C residue 187 type catalytic sequence R description 935 source MCSA : MCSA3 44) chain C residue 356 type catalytic sequence W description 935 source MCSA : MCSA3 45) chain C residue 361 type catalytic sequence E description 935 source MCSA : MCSA3 46) chain C residue 102 type BINDING sequence S description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 47) chain C residue 247 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 48) chain C residue 356 type BINDING sequence W description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 49) chain C residue 357 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 50) chain C residue 361 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 51) chain C residue 366 type BINDING sequence N description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 52) chain C residue 446 type BINDING sequence A description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 53) chain C residue 447 type BINDING sequence W description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 54) chain C residue 460 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 55) chain C residue 475 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 56) chain C residue 184 type BINDING sequence C description axial binding residue => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI3 57) chain C residue 365 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P source Swiss-Prot : SWS_FT_FI4 58) chain C residue 94 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:18849972, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:1M9J, ECO:0007744|PDB:1M9K, ECO:0007744|PDB:1M9M, ECO:0007744|PDB:1M9Q, ECO:0007744|PDB:1M9R, ECO:0007744|PDB:3EAH, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P source Swiss-Prot : SWS_FT_FI1 59) chain C residue 99 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:18849972, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:1M9J, ECO:0007744|PDB:1M9K, ECO:0007744|PDB:1M9M, ECO:0007744|PDB:1M9Q, ECO:0007744|PDB:1M9R, ECO:0007744|PDB:3EAH, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P source Swiss-Prot : SWS_FT_FI1

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