eF-site ID 1ooq-B PDB Code 1ooq Chain B click to enlarge Title Nitroreductase from e-coli in complex with the inhibitor dicoumarol Classification OXIDOREDUCTASE Compound Oxygen-insensitive NAD(P)H nitroreductase Source null (NFNB_ECOLI) Sequence B:  DIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSST NSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHV VVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGR KFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDA VPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNA TLPKSRLPQNITLTEV Description Functional site 1) chain B residue 38 type sequence P description BINDING SITE FOR RESIDUE FMN A 218 source : AC1 2) chain B residue 39 type sequence S description BINDING SITE FOR RESIDUE FMN A 218 source : AC1 3) chain B residue 40 type sequence S description BINDING SITE FOR RESIDUE FMN A 218 source : AC1 4) chain B residue 42 type sequence N description BINDING SITE FOR RESIDUE FMN A 218 source : AC1 5) chain B residue 142 type sequence Q description BINDING SITE FOR RESIDUE FMN A 218 source : AC1 6) chain B residue 145 type sequence L description BINDING SITE FOR RESIDUE FMN A 218 source : AC1 7) chain B residue 10 type sequence R description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 8) chain B residue 11 type sequence H description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 9) chain B residue 12 type sequence S description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 10) chain B residue 14 type sequence K description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 11) chain B residue 71 type sequence N description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 12) chain B residue 74 type sequence K description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 13) chain B residue 144 type sequence Y description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 14) chain B residue 163 type sequence P description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 15) chain B residue 164 type sequence I description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 16) chain B residue 165 type sequence E description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 17) chain B residue 166 type sequence G description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 18) chain B residue 205 type sequence K description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 19) chain B residue 207 type sequence R description BINDING SITE FOR RESIDUE FMN B 219 source : AC2 20) chain B residue 40 type sequence S description BINDING SITE FOR RESIDUE DTC B 222 source : AC3 21) chain B residue 41 type sequence T description BINDING SITE FOR RESIDUE DTC B 222 source : AC3 22) chain B residue 124 type sequence F description BINDING SITE FOR RESIDUE DTC B 222 source : AC3 23) chain B residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11020276, ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 165 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11020276, ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 205 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11020276, ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 14 type catalytic sequence K description 211 source MCSA : MCSA2 27) chain B residue 74 type catalytic sequence K description 211 source MCSA : MCSA2 28) chain B residue 165 type catalytic sequence E description 211 source MCSA : MCSA2 29) chain B residue 14 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q01234 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 107 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q01234 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 41 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q01234 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 71 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q01234 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 74 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q01234 source Swiss-Prot : SWS_FT_FI2

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