eF-site ID 1npx-A PDB Code 1npx Chain A click to enlarge Title STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION Classification OXIDOREDUCTASE(H2O2(A)) Compound NADH PEROXIDASE Source Enterococcus faecalis (Streptococcus faecalis) (NAPE_ENTFA) Sequence A:  MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFL SXGMQLYLEGKVKDVNSVRYMTGEKMESRGVNVFSNTEIT AIQPKEHQVTVKDLVSGEERVENYDKLIISPGAVPFELDI PGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYI GIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEE MEANNITIATGETVERYEGDGRVQKVVTDKNAYDADLVVV AVGVRPNTAWLKGTLELHPNGLIKTDEYMRTSEPDVFAVG DATLIKYNPADTEVNIALATNARKQGRFAVKNLEEPVKPF PGVQGSSGLAVFDYKFASTGINEVMAQKLGKETKAVTVVE DYLMDFNPDKQKAWFKLVYDPETTQILGAQLMSKADLTAN INAISLAIQAKMTIEDLAYADFFFQPAFDKPWNIINTAAL EAVKQER Description (1)  NADH PEROXIDASE (E.C.1.11.1.1) NON-ACTIVE FORM WITH CYS 42 OXIDIZED TO A SULFONIC ACID (CYS42-SO3H) Functional site 1) chain A residue 9 type sequence S description source : AC2 2) chain A residue 10 type sequence H description source : AC2 3) chain A residue 11 type sequence G description source : AC2 4) chain A residue 32 type sequence E description source : AC2 5) chain A residue 33 type sequence K description source : AC2 6) chain A residue 79 type sequence I description source : AC2 7) chain A residue 110 type sequence S description source : AC2 8) chain A residue 111 type sequence P description source : AC2 9) chain A residue 112 type sequence G description source : AC2 10) chain A residue 113 type sequence A description source : AC2 11) chain A residue 132 type sequence R description source : AC2 12) chain A residue 159 type sequence Y description source : AC2 13) chain A residue 247 type sequence N description source : AC2 14) chain A residue 280 type sequence G description source : AC2 15) chain A residue 281 type sequence D description source : AC2 16) chain A residue 297 type sequence A description source : AC2 17) chain A residue 298 type sequence L description source : AC2 18) chain A residue 299 type sequence A description source : AC2 19) chain A residue 424 type sequence F description source : AC2 20) chain A residue 6 type sequence L description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 21) chain A residue 7 type sequence G description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 22) chain A residue 9 type sequence S description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 23) chain A residue 10 type sequence H description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 24) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 25) chain A residue 32 type sequence E description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 26) chain A residue 33 type sequence K description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 27) chain A residue 41 type sequence S description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 28) chain A residue 42 type sequence X description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 29) chain A residue 78 type sequence E description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 30) chain A residue 79 type sequence I description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 31) chain A residue 110 type sequence S description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 32) chain A residue 111 type sequence P description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 33) chain A residue 112 type sequence G description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 34) chain A residue 113 type sequence A description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 35) chain A residue 132 type sequence R description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 36) chain A residue 159 type sequence Y description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 37) chain A residue 160 type sequence I description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 38) chain A residue 247 type sequence N description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 39) chain A residue 280 type sequence G description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 40) chain A residue 281 type sequence D description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 41) chain A residue 297 type sequence A description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 42) chain A residue 298 type sequence L description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 43) chain A residue 299 type sequence A description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 44) chain A residue 424 type sequence F description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 45) chain A residue 425 type sequence Q description BINDING SITE FOR RESIDUE FAD A 449 source : AC1 46) chain A residue 10 type catalytic sequence H description 895 source MCSA : MCSA1 47) chain A residue 41 type catalytic sequence S description 895 source MCSA : MCSA1 48) chain A residue 42 type catalytic sequence X description 895 source MCSA : MCSA1 49) chain A residue 303 type catalytic sequence R description 895 source MCSA : MCSA1 50) chain A residue 10 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 42 type ACT_SITE sequence X description Redox-active => ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 7 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 32 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI3 54) chain A residue 42 type BINDING sequence X description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI3 55) chain A residue 110 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI3 56) chain A residue 132 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 281 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 299 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 160 type BINDING sequence I description BINDING => ECO:0000269|PubMed:8425532 source Swiss-Prot : SWS_FT_FI4 60) chain A residue 179 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8425532 source Swiss-Prot : SWS_FT_FI4 61) chain A residue 188 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:8425532 source Swiss-Prot : SWS_FT_FI4 62) chain A residue 243 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8425532 source Swiss-Prot : SWS_FT_FI4 63) chain A residue 297 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8425532 source Swiss-Prot : SWS_FT_FI4 64) chain A residue 328 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8425532 source Swiss-Prot : SWS_FT_FI4 65) chain A residue 42 type MOD_RES sequence X description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:8756456 source Swiss-Prot : SWS_FT_FI5

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