eF-site ID 6bpr-A PDB Code 6bpr Chain A click to enlarge Title Crystal structure of cysteine, nitric oxide-bound ferrous form of the uncrosslinked F2-Tyr157 human cysteine dioxygenase Classification OXIDOREDUCTASE Compound Cysteine dioxygenase type 1 Source (CDO1_HUMAN) Sequence A:  EVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDP TEWAMYAKFDQYRYTRNLVDQGNGKFNLMILCWGEGHGSS IHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERV LRENQCAYINDSVGLHRVENISHTEPAVSLHLXSPPFDTC HAFDQRTGHKNKVTMTFHSKFGIRTP Description Functional site 1) chain A residue 86 type sequence H description binding site for residue FE A 301 source : AC1 2) chain A residue 88 type sequence H description binding site for residue FE A 301 source : AC1 3) chain A residue 140 type sequence H description binding site for residue FE A 301 source : AC1 4) chain A residue 58 type sequence Y description binding site for residue CYS A 302 source : AC2 5) chain A residue 60 type sequence R description binding site for residue CYS A 302 source : AC2 6) chain A residue 75 type sequence L description binding site for residue CYS A 302 source : AC2 7) chain A residue 86 type sequence H description binding site for residue CYS A 302 source : AC2 8) chain A residue 88 type sequence H description binding site for residue CYS A 302 source : AC2 9) chain A residue 140 type sequence H description binding site for residue CYS A 302 source : AC2 10) chain A residue 157 type sequence X description binding site for residue CYS A 302 source : AC2 11) chain A residue 179 type sequence M description binding site for residue CYS A 302 source : AC2 12) chain A residue 88 type sequence H description binding site for residue NO A 303 source : AC3 13) chain A residue 93 type sequence C description binding site for residue NO A 303 source : AC3 14) chain A residue 140 type sequence H description binding site for residue NO A 303 source : AC3 15) chain A residue 155 type sequence H description binding site for residue NO A 303 source : AC3 16) chain A residue 157 type sequence X description binding site for residue NO A 303 source : AC3 17) chain A residue 34 type sequence Q description binding site for residue SO4 A 304 source : AC4 18) chain A residue 123 type sequence R description binding site for residue SO4 A 304 source : AC4 19) chain A residue 131 type sequence A description binding site for residue SO4 A 304 source : AC4 20) chain A residue 132 type sequence Y description binding site for residue SO4 A 304 source : AC4 21) chain A residue 119 type sequence K description binding site for residue SO4 A 305 source : AC5 22) chain A residue 141 type sequence R description binding site for residue SO4 A 305 source : AC5 23) chain A residue 169 type sequence Q description binding site for residue SO4 A 305 source : AC5 24) chain A residue 56 type sequence Y description binding site for residue SO4 A 306 source : AC6 25) chain A residue 173 type sequence H description binding site for residue SO4 A 306 source : AC6 26) chain A residue 174 type sequence K description binding site for residue SO4 A 306 source : AC6 27) chain A residue 166 type sequence A description binding site for residue GOL A 307 source : AC7 28) chain A residue 168 type sequence D description binding site for residue GOL A 307 source : AC7 29) chain A residue 173 type sequence H description binding site for residue GOL A 307 source : AC7 30) chain A residue 175 type sequence N description binding site for residue GOL A 307 source : AC7 31) chain A residue 58 type sequence Y description binding site for residue GOL A 308 source : AC8 32) chain A residue 83 type sequence S description binding site for residue GOL A 308 source : AC8 33) chain A residue 84 type sequence S description binding site for residue GOL A 308 source : AC8 34) chain A residue 164 type sequence C description binding site for residue GOL A 308 source : AC8 35) chain A residue 165 type sequence H description binding site for residue GOL A 309 source : AC9 36) chain A residue 174 type sequence K description binding site for residue GOL A 309 source : AC9 37) chain A residue 42 type sequence S description binding site for residue GOL A 310 source : AD1 38) chain A residue 44 type sequence P description binding site for residue GOL A 310 source : AD1 39) chain A residue 98 type sequence L description binding site for residue GOL A 310 source : AD1 40) chain A residue 127 type sequence E description binding site for residue GOL A 310 source : AD1 41) chain A residue 101 type sequence N description binding site for residue GOL A 311 source : AD2 42) chain A residue 116 type sequence E description binding site for residue GOL A 311 source : AD2 43) chain A residue 117 type sequence M description binding site for residue GOL A 311 source : AD2 44) chain A residue 118 type sequence V description binding site for residue GOL A 311 source : AD2 45) chain A residue 126 type sequence R description binding site for residue GOL A 311 source : AD2 46) chain A residue 127 type sequence E description binding site for residue GOL A 311 source : AD2 47) chain A residue 180 type sequence T description binding site for residue GOL A 312 source : AD3 48) chain A residue 181 type sequence F description binding site for residue GOL A 312 source : AD3 49) chain A residue 184 type sequence K description binding site for residue GOL A 312 source : AD3 50) chain A residue 8 type sequence K description binding site for residue GOL A 313 source : AD4 51) chain A residue 10 type sequence R description binding site for residue GOL A 313 source : AD4 52) chain A residue 86 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17135237 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 88 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17135237 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 140 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17135237 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 157 type CROSSLNK sequence X description 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) => ECO:0000269|PubMed:17135237 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 93 type CROSSLNK sequence C description 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) => ECO:0000269|PubMed:17135237 source Swiss-Prot : SWS_FT_FI2

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