eF-site ID 1j2g-ABCD PDB Code 1j2g Chain A, B, C, D click to enlarge Title Crystal structure of Urate oxidase from Bacillus SP. TB-90 co-crystallized with 8-Azaxanthine Classification OXIDOREDUCTASE Compound Uricase Source null (URIC_BACSB) Sequence A:  RVMYYGKGDVFAYRTYLKPLTGVRTIPESPFSGRDHILFG VNVKISVGGTKLLTSFTKGDNSLVVATDSMKNFIQKHLAS YTGTTIEGFLEYVATSFLKKYSHIEKISLIGEEIPFETTF AVKNGNRAASELVFKKSRNEYATAYLNMVRNEDNTLNITE QQSGLAGLQLIKVSGNSFVGFIRDEYTTLPEDSNRPLFVY LNIKWKYKNTEDSFGTNPENYVAAEQIRDIATSVFHETET LSIQHLIYLIGRRILERFPQLQEVYFESQNHTWDKIVEEI PESEGKVYTEPRPPYGFQCFTVTQED B:  RVMYYGKGDVFAYRTYLKPLTGVRTIPESPFSGRDHILFG VNVKISVGGTKLLTSFTKGDNSLVVATDSMKNFIQKHLAS YTGTTIEGFLEYVATSFLKKYSHIEKISLIGEEIPFETTF AVKNGNRAASELVFKKSRNEYATAYLNMVRNEDNTLNITE QQSGLAGLQLIKVSGNSFVGFIRDEYTTLPEDSNRPLFVY LNIKWKYKNTEDSFGTNPENYVAAEQIRDIATSVFHETET LSIQHLIYLIGRRILERFPQLQEVYFESQNHTWDKIVEEI PESEGKVYTEPRPPYGFQCFTVTQED C:  RVMYYGKGDVFAYRTYLKPLTGVRTIPESPFSGRDHILFG VNVKISVGGTKLLTSFTKGDNSLVVATDSMKNFIQKHLAS YTGTTIEGFLEYVATSFLKKYSHIEKISLIGEEIPFETTF AVKNGNRAASELVFKKSRNEYATAYLNMVRNEDNTLNITE QQSGLAGLQLIKVSGNSFVGFIRDEYTTLPEDSNRPLFVY LNIKWKYKNTEDSFGTNPENYVAAEQIRDIATSVFHETET LSIQHLIYLIGRRILERFPQLQEVYFESQNHTWDKIVEEI PESEGKVYTEPRPPYGFQCFTVTQED D:  RVMYYGKGDVFAYRTYLKPLTGVRTIPESPFSGRDHILFG VNVKISVGGTKLLTSFTKGDNSLVVATDSMKNFIQKHLAS YTGTTIEGFLEYVATSFLKKYSHIEKISLIGEEIPFETTF AVKNGNRAASELVFKKSRNEYATAYLNMVRNEDNTLNITE QQSGLAGLQLIKVSGNSFVGFIRDEYTTLPEDSNRPLFVY LNIKWKYKNTEDSFGTNPENYVAAEQIRDIATSVFHETET LSIQHLIYLIGRRILERFPQLQEVYFESQNHTWDKIVEEI PESEGKVYTEPRPPYGFQCFTVTQED Description Functional site 1) chain B residue 298 type sequence R description BINDING SITE FOR RESIDUE SO4 B 501 source : AC1 2) chain D residue 298 type sequence R description BINDING SITE FOR RESIDUE SO4 B 501 source : AC1 3) chain A residue 106 type sequence K description BINDING SITE FOR RESIDUE SO4 A 502 source : AC2 4) chain A residue 190 type sequence D description BINDING SITE FOR RESIDUE SO4 A 502 source : AC2 5) chain A residue 191 type sequence E description BINDING SITE FOR RESIDUE SO4 A 502 source : AC2 6) chain B residue 106 type sequence K description BINDING SITE FOR RESIDUE SO4 A 502 source : AC2 7) chain A residue 31 type sequence T description BINDING SITE FOR RESIDUE SO4 D 503 source : AC3 8) chain A residue 31 type sequence T description BINDING SITE FOR RESIDUE SO4 D 503 source : AC3 9) chain D residue 133 type sequence R description BINDING SITE FOR RESIDUE SO4 D 503 source : AC3 10) chain D residue 133 type sequence R description BINDING SITE FOR RESIDUE SO4 D 503 source : AC3 11) chain A residue 298 type sequence R description BINDING SITE FOR RESIDUE SO4 A 504 source : AC4 12) chain C residue 298 type sequence R description BINDING SITE FOR RESIDUE SO4 A 504 source : AC4 13) chain A residue 184 type sequence F description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 14) chain A residue 195 type sequence L description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 15) chain A residue 201 type sequence R description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 16) chain A residue 248 type sequence S description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 17) chain A residue 249 type sequence I description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 18) chain A residue 250 type sequence Q description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 19) chain A residue 276 type sequence N description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 20) chain B residue 11 type sequence Y description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 21) chain B residue 72 type sequence A description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 22) chain B residue 73 type sequence T description BINDING SITE FOR RESIDUE AZA A 4320 source : AC5 23) chain A residue 11 type sequence Y description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 24) chain A residue 72 type sequence A description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 25) chain A residue 73 type sequence T description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 26) chain B residue 184 type sequence F description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 27) chain B residue 195 type sequence L description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 28) chain B residue 201 type sequence R description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 29) chain B residue 248 type sequence S description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 30) chain B residue 249 type sequence I description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 31) chain B residue 250 type sequence Q description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 32) chain B residue 276 type sequence N description BINDING SITE FOR RESIDUE AZA B 1320 source : AC6 33) chain C residue 184 type sequence F description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 34) chain C residue 201 type sequence R description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 35) chain C residue 248 type sequence S description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 36) chain C residue 249 type sequence I description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 37) chain C residue 250 type sequence Q description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 38) chain C residue 276 type sequence N description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 39) chain D residue 11 type sequence Y description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 40) chain D residue 72 type sequence A description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 41) chain D residue 73 type sequence T description BINDING SITE FOR RESIDUE AZA C 2320 source : AC7 42) chain C residue 73 type sequence T description BINDING SITE FOR RESIDUE AZA D 3320 source : AC8 43) chain D residue 184 type sequence F description BINDING SITE FOR RESIDUE AZA D 3320 source : AC8 44) chain D residue 195 type sequence L description BINDING SITE FOR RESIDUE AZA D 3320 source : AC8 45) chain D residue 201 type sequence R description BINDING SITE FOR RESIDUE AZA D 3320 source : AC8 46) chain D residue 248 type sequence S description BINDING SITE FOR RESIDUE AZA D 3320 source : AC8 47) chain D residue 249 type sequence I description BINDING SITE FOR RESIDUE AZA D 3320 source : AC8 48) chain D residue 250 type sequence Q description BINDING SITE FOR RESIDUE AZA D 3320 source : AC8 49) chain D residue 276 type sequence N description BINDING SITE FOR RESIDUE AZA D 3320 source : AC8 50) chain A residue 73 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 276 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 52) chain C residue 73 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 53) chain C residue 74 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 54) chain C residue 249 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 55) chain C residue 250 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 56) chain C residue 276 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 57) chain D residue 73 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 58) chain D residue 74 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 59) chain D residue 249 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 60) chain D residue 250 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 61) chain A residue 74 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 62) chain D residue 276 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 63) chain A residue 249 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 64) chain A residue 250 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 65) chain A residue 276 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 66) chain B residue 73 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 67) chain B residue 74 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 68) chain B residue 249 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 69) chain B residue 250 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI3 70) chain A residue 184 type BINDING sequence F description BINDING => ECO:0000305|Ref.3 source Swiss-Prot : SWS_FT_FI4 71) chain A residue 201 type BINDING sequence R description BINDING => ECO:0000305|Ref.3 source Swiss-Prot : SWS_FT_FI4 72) chain B residue 184 type BINDING sequence F description BINDING => ECO:0000305|Ref.3 source Swiss-Prot : SWS_FT_FI4 73) chain B residue 201 type BINDING sequence R description BINDING => ECO:0000305|Ref.3 source Swiss-Prot : SWS_FT_FI4 74) chain C residue 184 type BINDING sequence F description BINDING => ECO:0000305|Ref.3 source Swiss-Prot : SWS_FT_FI4 75) chain C residue 201 type BINDING sequence R description BINDING => ECO:0000305|Ref.3 source Swiss-Prot : SWS_FT_FI4 76) chain D residue 184 type BINDING sequence F description BINDING => ECO:0000305|Ref.3 source Swiss-Prot : SWS_FT_FI4 77) chain D residue 201 type BINDING sequence R description BINDING => ECO:0000305|Ref.3 source Swiss-Prot : SWS_FT_FI4 78) chain A residue 73 type ACT_SITE sequence T description Charge relay system; for urate oxidase activity => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 79) chain B residue 13 type ACT_SITE sequence K description Charge relay system; for urate oxidase activity => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 80) chain B residue 73 type ACT_SITE sequence T description Charge relay system; for urate oxidase activity => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 81) chain C residue 13 type ACT_SITE sequence K description Charge relay system; for urate oxidase activity => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 82) chain C residue 73 type ACT_SITE sequence T description Charge relay system; for urate oxidase activity => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 83) chain D residue 13 type ACT_SITE sequence K description Charge relay system; for urate oxidase activity => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 84) chain D residue 73 type ACT_SITE sequence T description Charge relay system; for urate oxidase activity => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 85) chain A residue 13 type ACT_SITE sequence K description Charge relay system; for urate oxidase activity => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 86) chain A residue 174-201 type prosite sequence LQLIKVSGNSFVGFIRDEYTTLPEDSNR description URICASE Uricase signature. LqLIKVSgNsFvgFirdeYttLpedsnR source prosite : PS00366 87) chain C residue 24 type ACT_SITE sequence K description Charge relay system => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 88) chain D residue 24 type ACT_SITE sequence K description Charge relay system => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 89) chain A residue 24 type ACT_SITE sequence K description Charge relay system => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 90) chain B residue 24 type ACT_SITE sequence K description Charge relay system => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2

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