eF-site ID 1r35-B PDB Code 1r35 Chain B click to enlarge Title MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER, TETRAHYDROBIOPTERIN AND 4R-FLUORO-N6-ETHANIMIDOYL-L-LYSINE Classification OXIDOREDUCTASE Compound Nitric oxide synthase, inducible Source Mus musculus (Mouse) (NOS2_MOUSE) Sequence B:  QYVRIKNWGSGEILHDTLHHKATSSCLGSIMNPKSLTRGP RDKPTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAV TKEIETTGTYQLTLDELIFATKMAWRNAPRCIGRIQWSNL QVFDARNCSTAQEMFQHICRHILYATNNGNIRSAITVFPQ RSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQL CIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEV TMEHPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPF NGWYMGTEIGVRDFCDTQRYNILEEVGRRMGLETHTLASL WKDRAVTEINVAVLHSFQKQNVTIMDHHTASESFMKHMQN EYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFY YYQIEPWKTHIWQ Description Functional site 1) chain B residue 188 type sequence W description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 2) chain B residue 193 type sequence R description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 3) chain B residue 194 type sequence C description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 4) chain B residue 195 type sequence I description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 5) chain B residue 236 type sequence S description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 6) chain B residue 349 type sequence M description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 7) chain B residue 363 type sequence F description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 8) chain B residue 364 type sequence N description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 9) chain B residue 365 type sequence G description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 10) chain B residue 366 type sequence W description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 11) chain B residue 371 type sequence E description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 12) chain B residue 457 type sequence W description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 13) chain B residue 485 type sequence Y description BINDING SITE FOR RESIDUE HEM B 901 source : AC5 14) chain B residue 112 type sequence S description BINDING SITE FOR RESIDUE H4B B 1902 source : AC6 15) chain B residue 114 type sequence M description BINDING SITE FOR RESIDUE H4B B 1902 source : AC6 16) chain B residue 375 type sequence R description BINDING SITE FOR RESIDUE H4B B 1902 source : AC6 17) chain B residue 455 type sequence W description BINDING SITE FOR RESIDUE H4B B 1902 source : AC6 18) chain B residue 456 type sequence I description BINDING SITE FOR RESIDUE H4B B 1902 source : AC6 19) chain B residue 457 type sequence W description BINDING SITE FOR RESIDUE H4B B 1902 source : AC6 20) chain B residue 470 type sequence F description BINDING SITE FOR RESIDUE H4B B 1902 source : AC6 21) chain B residue 471 type sequence H description BINDING SITE FOR RESIDUE H4B B 1902 source : AC6 22) chain B residue 257 type sequence Q description BINDING SITE FOR RESIDUE I58 B 1800 source : AC7 23) chain B residue 341 type sequence Y description BINDING SITE FOR RESIDUE I58 B 1800 source : AC7 24) chain B residue 344 type sequence P description BINDING SITE FOR RESIDUE I58 B 1800 source : AC7 25) chain B residue 346 type sequence V description BINDING SITE FOR RESIDUE I58 B 1800 source : AC7 26) chain B residue 366 type sequence W description BINDING SITE FOR RESIDUE I58 B 1800 source : AC7 27) chain B residue 367 type sequence Y description BINDING SITE FOR RESIDUE I58 B 1800 source : AC7 28) chain B residue 371 type sequence E description BINDING SITE FOR RESIDUE I58 B 1800 source : AC7 29) chain B residue 376 type sequence D description BINDING SITE FOR RESIDUE I58 B 1800 source : AC7 30) chain B residue 257 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI4 31) chain B residue 366 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI4 32) chain B residue 367 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI4 33) chain B residue 371 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P29474 source Swiss-Prot : SWS_FT_FI4 34) chain B residue 375 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1JWK, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:3NOD source Swiss-Prot : SWS_FT_FI5 35) chain B residue 456 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N source Swiss-Prot : SWS_FT_FI6 36) chain B residue 457 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD source Swiss-Prot : SWS_FT_FI7 37) chain B residue 470 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1JWK, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD source Swiss-Prot : SWS_FT_FI8 38) chain B residue 485 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD source Swiss-Prot : SWS_FT_FI9 39) chain B residue 112 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD source Swiss-Prot : SWS_FT_FI2 40) chain B residue 109 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:12464241, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWV, ECO:0007744|PDB:1DWW, ECO:0007744|PDB:1N2N source Swiss-Prot : SWS_FT_FI1 41) chain B residue 194 type BINDING sequence C description axial binding residue => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9334294, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWV, ECO:0007744|PDB:1DWW, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1JWK, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOC, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1NOS, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:2NOS, ECO:0007744|PDB:3NOD source Swiss-Prot : SWS_FT_FI3

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