eF-site ID 1n0i-A PDB Code 1n0i Chain A click to enlarge Title Crystal Structure of Ferrochelatase with Cadmium bound at active site Classification LYASE Compound Ferrochelatase Source Bacillus subtilis (strain 168) (HEMH_BACSU) Sequence A:  SRKKMGLLVMAYGTPYKEEDIERYYTHIRRGRKPEPEMLQ DLKDRYEAIGGISPLAQITEQQAHNLEQHLNEIQDEITFK AYIGLKHIEPFIEDAVAEMHKDGITEAVSIVLAPHFSTFS VQSYNKRAKEEAEKLGGLTITSVESWYDEPKFVTYWVDRV KETYASMPEDERENAMLIVSAHSLPEKIKEFGDPYPDQLH ESAKLIAEGAGVSEYAVGWQSEGNTPDPWLGPDVQDLTRD LFEQKGYQAFVYVPVGFVADHLEVLYDNDYECKVVTDDIG ASYYRPEMPNAKPEFIDALATVVLKKLGR Description Functional site 1) chain A residue 13 type sequence Y description BINDING SITE FOR RESIDUE CD A 910 source : AC1 2) chain A residue 183 type sequence H description BINDING SITE FOR RESIDUE CD A 910 source : AC1 3) chain A residue 222 type sequence S description BINDING SITE FOR RESIDUE CD A 910 source : AC1 4) chain A residue 264 type sequence E description BINDING SITE FOR RESIDUE CD A 910 source : AC1 5) chain A residue 262 type sequence H description BINDING SITE FOR RESIDUE CD A 911 source : AC2 6) chain A residue 145 type sequence E description BINDING SITE FOR RESIDUE CL A 912 source : AC3 7) chain A residue 307 type sequence K description BINDING SITE FOR RESIDUE CL A 912 source : AC3 8) chain A residue 33 type sequence R description BINDING SITE FOR RESIDUE CL A 913 source : AC4 9) chain A residue 117 type sequence F description BINDING SITE FOR RESIDUE CL A 913 source : AC4 10) chain A residue 146 type sequence S description BINDING SITE FOR RESIDUE CL A 913 source : AC4 11) chain A residue 199 type sequence Q description BINDING SITE FOR RESIDUE CL A 913 source : AC4 12) chain A residue 20 type sequence E description BINDING SITE FOR RESIDUE MG A 902 source : AC7 13) chain A residue 20 type BINDING sequence E description BINDING => ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 30 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00323 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 54 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00323 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 125 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_00323 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 264 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000305|PubMed:12761666, ECO:0000305|PubMed:16140324, ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751 source Swiss-Prot : SWS_FT_FI5 18) chain A residue 13 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10704318, ECO:0007744|PDB:1C1H source Swiss-Prot : SWS_FT_FI1 19) chain A residue 31 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10704318, ECO:0007744|PDB:1C1H source Swiss-Prot : SWS_FT_FI1 20) chain A residue 183 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10704318, ECO:0007744|PDB:1C1H source Swiss-Prot : SWS_FT_FI1 21) chain A residue 188 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10704318, ECO:0007744|PDB:1C1H source Swiss-Prot : SWS_FT_FI1 22) chain A residue 46 type BINDING sequence R description BINDING => ECO:0000305|PubMed:12761666 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 268 type BINDING sequence D description BINDING => ECO:0000305|PubMed:12761666 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 272 type BINDING sequence E description BINDING => ECO:0000305|PubMed:12761666 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 178-196 type prosite sequence LIVSAHSLPEKIKEFGDPY description FERROCHELATASE Ferrochelatase signature. LIvSaHSLPekik.EfGDp...Y source prosite : PS00534

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