eF-site ID 2bgj-ABCD PDB Code 2bgj Chain A, B, C, D click to enlarge Title X-Ray Structure of the Ferredoxin-NADP(H) Reductase from Rhodobacter capsulatus at 2.1 Angstroms Classification OXIDOREDUCTASE Compound FERREDOXIN-NADP(H) REDUCTASE Source (Q9L6V3) Sequence A:  KVLPDAQTVTSVRHWTDTLFSFRVTRPQTLRFRSGEFVMI GLLDDNGKPIMRAYSIASPAWDEELEFYSIKVPDGPLTSR LQHIKVGEQIILRPKPVGTLVIDALLPGKRLWFLATGTGI APFASLMREPEAYEKFDEVIMMHACRTVAELEYGRQLVEA LQEDPLIGELVEGKLKYYPTTTREEFHHMGRITDNLASGK VFEDLGIAPMNPETDRAMVCGSLAFNVDVMKVLESYGLRE GANSEPREFVVEKAFVGEGI B:  PDAQTVTSVRHWTDTLFSFRVTRPQTLRFRSGEFVMIGLL DDNGKPIMRAYSIASPAWDEELEFYSIKVPDGPLTSRLQH IKVGEQIILRPKPVGTLVIDALLPGKRLWFLATGTGIAPF ASLMREPEAYEKFDEVIMMHACRTVAELEYGRQLVEALQE DPLIGELVEGKLKYYPTTTREEFHHMGRITDNLASGKVFE DLGIAPMNPETDRAMVCGSLAFNVDVMKVLESYGLREGAN SEPREFVVEKAFVGEGI C:  PDAQTVTSVRHWTDTLFSFRVTRPQTLRFRSGEFVMIGLL DDNGKPIMRAYSIASPAWDEELEFYSIKVPDGPLTSRLQH IKVGEQIILRPKPVGTLVIDALLPGKRLWFLATGTGIAPF ASLMREPEAYEKFDEVIMMHACRTVAELEYGRQLVEALQE DPLIGELVEGKLKYYPTTTREEFHHMGRITDNLASGKVFE DLGIAPMNPETDRAMVCGSLAFNVDVMKVLESYGLREGAN SEPREFVVEKAFVGEGI D:  PDAQTVTSVRHWTDTLFSFRVTRPQTLRFRSGEFVMIGLL DDNGKPIMRAYSIASPAWDEELEFYSIKVPDGPLTSRLQH IKVGEQIILRPKPVGTLVIDALLPGKRLWFLATGTGIAPF ASLMREPEAYEKFDEVIMMHACRTVAELEYGRQLVEALQE DPLIGELVEGKLKYYPTTTREEFHHMGRITDNLASGKVFE DLGIAPMNPETDRAMVCGSLAFNVDVMKVLESYGLREGAN SEPREFVVEKAFVGEGI Description Functional site 1) chain A residue 49 type sequence F description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 2) chain A residue 64 type sequence R description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 3) chain A residue 65 type sequence A description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 4) chain A residue 66 type sequence Y description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 5) chain A residue 67 type sequence S description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 6) chain A residue 80 type sequence Y description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 7) chain A residue 81 type sequence S description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 8) chain A residue 82 type sequence I description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 9) chain A residue 84 type sequence V description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 10) chain A residue 87 type sequence G description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 11) chain A residue 88 type sequence P description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 12) chain A residue 89 type sequence L description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 13) chain A residue 90 type sequence T description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 14) chain A residue 130 type sequence T description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 15) chain A residue 133 type sequence A description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 16) chain A residue 265 type sequence K description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 17) chain A residue 266 type sequence A description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 18) chain A residue 267 type sequence F description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 19) chain A residue 271 type sequence G description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 20) chain A residue 272 type sequence I description BINDING SITE FOR RESIDUE FAD A1273 source : AC1 21) chain B residue 49 type sequence F description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 22) chain B residue 64 type sequence R description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 23) chain B residue 65 type sequence A description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 24) chain B residue 66 type sequence Y description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 25) chain B residue 67 type sequence S description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 26) chain B residue 80 type sequence Y description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 27) chain B residue 81 type sequence S description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 28) chain B residue 82 type sequence I description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 29) chain B residue 87 type sequence G description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 30) chain B residue 88 type sequence P description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 31) chain B residue 89 type sequence L description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 32) chain B residue 90 type sequence T description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 33) chain B residue 130 type sequence T description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 34) chain B residue 133 type sequence A description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 35) chain B residue 265 type sequence K description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 36) chain B residue 266 type sequence A description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 37) chain B residue 267 type sequence F description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 38) chain B residue 268 type sequence V description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 39) chain B residue 270 type sequence E description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 40) chain B residue 271 type sequence G description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 41) chain B residue 272 type sequence I description BINDING SITE FOR RESIDUE FAD B1273 source : AC2 42) chain C residue 64 type sequence R description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 43) chain C residue 65 type sequence A description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 44) chain C residue 66 type sequence Y description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 45) chain C residue 67 type sequence S description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 46) chain C residue 80 type sequence Y description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 47) chain C residue 81 type sequence S description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 48) chain C residue 82 type sequence I description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 49) chain C residue 84 type sequence V description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 50) chain C residue 87 type sequence G description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 51) chain C residue 88 type sequence P description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 52) chain C residue 89 type sequence L description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 53) chain C residue 90 type sequence T description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 54) chain C residue 130 type sequence T description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 55) chain C residue 133 type sequence A description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 56) chain C residue 265 type sequence K description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 57) chain C residue 266 type sequence A description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 58) chain C residue 267 type sequence F description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 59) chain C residue 268 type sequence V description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 60) chain C residue 270 type sequence E description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 61) chain C residue 271 type sequence G description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 62) chain C residue 272 type sequence I description BINDING SITE FOR RESIDUE FAD C1273 source : AC3 63) chain D residue 64 type sequence R description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 64) chain D residue 65 type sequence A description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 65) chain D residue 66 type sequence Y description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 66) chain D residue 67 type sequence S description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 67) chain D residue 80 type sequence Y description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 68) chain D residue 81 type sequence S description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 69) chain D residue 82 type sequence I description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 70) chain D residue 87 type sequence G description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 71) chain D residue 88 type sequence P description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 72) chain D residue 89 type sequence L description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 73) chain D residue 90 type sequence T description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 74) chain D residue 130 type sequence T description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 75) chain D residue 133 type sequence A description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 76) chain D residue 265 type sequence K description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 77) chain D residue 266 type sequence A description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 78) chain D residue 267 type sequence F description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 79) chain D residue 268 type sequence V description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 80) chain D residue 270 type sequence E description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 81) chain D residue 271 type sequence G description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 82) chain D residue 272 type sequence I description BINDING SITE FOR RESIDUE FAD D1273 source : AC4 83) chain A residue 64 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 84) chain C residue 80 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 85) chain C residue 88 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 86) chain C residue 130 type BINDING sequence T description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 87) chain D residue 64 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 88) chain D residue 80 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 89) chain D residue 88 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 90) chain D residue 130 type BINDING sequence T description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 91) chain A residue 80 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 92) chain A residue 88 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 93) chain A residue 130 type BINDING sequence T description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 94) chain B residue 64 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 95) chain B residue 80 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 96) chain B residue 88 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 97) chain B residue 130 type BINDING sequence T description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 98) chain C residue 64 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 source Swiss-Prot : SWS_FT_FI1 99) chain A residue 128 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 100) chain B residue 240 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 101) chain C residue 128 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 102) chain C residue 158 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 103) chain C residue 194 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 104) chain C residue 203 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 105) chain C residue 240 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 106) chain D residue 128 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 107) chain D residue 158 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 108) chain D residue 194 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 109) chain D residue 203 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 110) chain A residue 158 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 111) chain D residue 240 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 112) chain A residue 194 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 113) chain A residue 203 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 114) chain A residue 240 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 115) chain B residue 128 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 116) chain B residue 158 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 117) chain B residue 194 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 118) chain B residue 203 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI2 119) chain A residue 266 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI3 120) chain B residue 266 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI3 121) chain C residue 266 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI3 122) chain D residue 266 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834 source Swiss-Prot : SWS_FT_FI3

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