eF-site ID 4z7y-ABCDEF PDB Code 4z7y Chain A, B, C, D, E, F click to enlarge Title diphosphomevalonate decarboxylase from the Sulfolobus solfataricus, space group P21 Classification LYASE Compound Diphosphomevalonate decarboxylase Source (DMD_SULSO) Sequence A:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV LSRE B:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV LSRE C:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV LSRE D:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV LSRE E:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV LSRE F:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV LSRE Description Functional site 1) chain A residue 148 type sequence G description binding site for residue SO4 A 401 source : AC1 2) chain A residue 149 type sequence G description binding site for residue SO4 A 401 source : AC1 3) chain A residue 168 type sequence Q description binding site for residue SO4 A 401 source : AC1 4) chain A residue 172 type sequence H description binding site for residue SO4 A 401 source : AC1 5) chain A residue 317 type sequence D description binding site for residue SO4 A 401 source : AC1 6) chain A residue 318 type sequence G description binding site for residue SO4 A 401 source : AC1 7) chain B residue 148 type sequence G description binding site for residue SO4 B 401 source : AC2 8) chain B residue 149 type sequence G description binding site for residue SO4 B 401 source : AC2 9) chain B residue 168 type sequence Q description binding site for residue SO4 B 401 source : AC2 10) chain B residue 171 type sequence R description binding site for residue SO4 B 401 source : AC2 11) chain B residue 172 type sequence H description binding site for residue SO4 B 401 source : AC2 12) chain B residue 317 type sequence D description binding site for residue SO4 B 401 source : AC2 13) chain B residue 318 type sequence G description binding site for residue SO4 B 401 source : AC2 14) chain C residue 148 type sequence G description binding site for residue SO4 C 401 source : AC3 15) chain C residue 149 type sequence G description binding site for residue SO4 C 401 source : AC3 16) chain C residue 168 type sequence Q description binding site for residue SO4 C 401 source : AC3 17) chain C residue 171 type sequence R description binding site for residue SO4 C 401 source : AC3 18) chain C residue 172 type sequence H description binding site for residue SO4 C 401 source : AC3 19) chain D residue 148 type sequence G description binding site for residue SO4 D 401 source : AC4 20) chain D residue 149 type sequence G description binding site for residue SO4 D 401 source : AC4 21) chain D residue 168 type sequence Q description binding site for residue SO4 D 401 source : AC4 22) chain D residue 172 type sequence H description binding site for residue SO4 D 401 source : AC4 23) chain D residue 317 type sequence D description binding site for residue SO4 D 401 source : AC4 24) chain D residue 318 type sequence G description binding site for residue SO4 D 401 source : AC4 25) chain E residue 148 type sequence G description binding site for residue SO4 E 401 source : AC5 26) chain E residue 149 type sequence G description binding site for residue SO4 E 401 source : AC5 27) chain E residue 168 type sequence Q description binding site for residue SO4 E 401 source : AC5 28) chain E residue 172 type sequence H description binding site for residue SO4 E 401 source : AC5 29) chain E residue 317 type sequence D description binding site for residue SO4 E 401 source : AC5 30) chain E residue 318 type sequence G description binding site for residue SO4 E 401 source : AC5 31) chain F residue 148 type sequence G description binding site for residue SO4 F 401 source : AC6 32) chain F residue 168 type sequence Q description binding site for residue SO4 F 401 source : AC6 33) chain F residue 171 type sequence R description binding site for residue SO4 F 401 source : AC6 34) chain F residue 172 type sequence H description binding site for residue SO4 F 401 source : AC6 35) chain F residue 317 type sequence D description binding site for residue SO4 F 401 source : AC6 36) chain F residue 318 type sequence G description binding site for residue SO4 F 401 source : AC6 37) chain A residue 121-128 type prosite sequence LLELNLKS description CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLELNLKS source prosite : PS00867 38) chain A residue 18 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 39) chain D residue 18 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 40) chain D residue 75 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 139 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 42) chain E residue 18 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 43) chain E residue 75 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 44) chain E residue 139 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 45) chain F residue 18 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 46) chain F residue 75 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 47) chain F residue 139 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 75 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 139 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 50) chain B residue 18 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 75 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 139 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 53) chain C residue 18 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 54) chain C residue 75 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1 55) chain C residue 139 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O23722 source Swiss-Prot : SWS_FT_FI1

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