eF-site ID 1bl9-A PDB Code 1bl9 Chain A click to enlarge Title CONFORMATIONAL CHANGES OCCURRING UPON REDUCTION IN NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA Classification OXIDOREDUCTASE Compound NITRITE REDUCTASE Source ORGANISM_SCIENTIFIC: Pseudomonas aeruginosa; Sequence A:  AEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQR CAGCHGVLRKGATGKPLTPDITQQRGQQYLEALITYGTPL GMPNWGSSGELSKEQITLMAKYIQHTPPQPPEWGMPEMRE SWKVLVKPEDRPKKQLNDLDLPNLFSVTLRDAGQIALVDG DSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMID LWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYW PPQFAIMDGETLEPKQIVSTRGMTVDTQTYHPEPRVAAII ASHEHPEFIVNVKETGKVLLVNYKDIDNLTVTSIGAAPFL HDGGWDSSHRYFMTAANNSNKVAVIDSKDRRLSALVDVGK TPHPGRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNHP QYAWKKVAELQGQGGGSLFIKTHPKSSHLYVDTTFNPDAR ISQSVAVFDLKNLDAKYQVLPIAEWADLGEGAKRVVQPEY NKRGDEVWFSVWNGKNDSSALVVVDDKTLKLKAVVKDPRL ITPTGKFNVYNTQHDVY Description (1)  NITRITE REDUCTASE, HEME C, HEME D Functional site 1) chain A residue 327 type sequence H description CATALYTIC SITE ON SUBUNIT A source : CSA 2) chain A residue 369 type sequence H description CATALYTIC SITE ON SUBUNIT A source : CSA 3) chain A residue 46 type sequence R description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 4) chain A residue 47 type sequence C description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 5) chain A residue 50 type sequence C description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 6) chain A residue 51 type sequence H description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 7) chain A residue 59 type sequence T description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 8) chain A residue 60 type sequence G description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 9) chain A residue 61 type sequence K description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 10) chain A residue 71 type sequence R description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 11) chain A residue 76 type sequence L description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 12) chain A residue 79 type sequence L description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 13) chain A residue 84 type sequence T description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 14) chain A residue 86 type sequence L description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 15) chain A residue 87 type sequence G description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 16) chain A residue 88 type sequence M description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 17) chain A residue 89 type sequence P description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 18) chain A residue 91 type sequence W description BINDING SITE FOR RESIDUE HEC A 601 source : AC2 19) chain A residue 156 type sequence R description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 20) chain A residue 182 type sequence H description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 21) chain A residue 183 type sequence I description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 22) chain A residue 185 type sequence R description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 23) chain A residue 198 type sequence R description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 24) chain A residue 225 type sequence R description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 25) chain A residue 226 type sequence S description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 26) chain A residue 245 type sequence Y description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 27) chain A residue 283 type sequence A description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 28) chain A residue 284 type sequence A description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 29) chain A residue 285 type sequence I description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 30) chain A residue 327 type sequence H description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 31) chain A residue 372 type sequence R description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 32) chain A residue 425 type sequence F description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 33) chain A residue 483 type sequence Q description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 34) chain A residue 531 type sequence G description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 35) chain A residue 533 type sequence F description BINDING SITE FOR RESIDUE DHE A 602 source : AC3 36) chain A residue 8 type sequence E description BINDING SITE FOR RESIDUE HEC B 601 source : AC4 37) chain A residue 10 type sequence Y description BINDING SITE FOR RESIDUE DHE B 602 source : AC5 38) chain A residue 13 type sequence A description BINDING SITE FOR RESIDUE DHE B 602 source : AC5 39) chain A residue 47 type catalytic sequence C description 903 source MCSA : MCSA1 40) chain A residue 50 type catalytic sequence C description 903 source MCSA : MCSA1 41) chain A residue 51 type catalytic sequence H description 903 source MCSA : MCSA1 42) chain A residue 88 type catalytic sequence M description 903 source MCSA : MCSA1 43) chain A residue 327 type catalytic sequence H description 903 source MCSA : MCSA1 44) chain A residue 369 type catalytic sequence H description 903 source MCSA : MCSA1 45) chain A residue 225 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI3 46) chain A residue 226 type BINDING sequence S description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI3 47) chain A residue 245 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI3 48) chain A residue 372 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI3 49) chain A residue 483 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI3 50) chain A residue 71 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI3 51) chain A residue 84 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI3 52) chain A residue 182 type BINDING sequence H description proximal binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI4 53) chain A residue 50 type BINDING sequence C description covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI1 54) chain A residue 47 type BINDING sequence C description covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI1 55) chain A residue 51 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI2 56) chain A residue 88 type BINDING sequence M description axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR source Swiss-Prot : SWS_FT_FI2

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