eF-site ID 6rkg-BC PDB Code 6rkg Chain B, C click to enlarge Title 1.32 A RESOLUTION OF SPOROSARCINA PASTEURII UREASE INHIBITED IN THE PRESENCE OF NBPTO AT pH 7.5 Classification HYDROLASE Compound Urease subunit gamma Source ORGANISM_SCIENTIFIC: Sporosarcina pasteurii; Sequence B:  NYIVPGEYRVAEGEIEINAGREKTTIRVSNTGDRPIQVGS HIHFVEVNKELLFDRAEGIGRRLNIPSGTAARFEPGEEME VELTELGGNREVFGISDLTNGSVDNKELILQRAKELGYKG VE C:  MKINRQQYAESYGPTVGDQVRLADTDLWIEVEKDYTTYGD EANFGGGKVLREGMGENGTYTRTENVLDLLLTNALILDYT GIYKADIGVKDGYIVGIGKGGNPDIMDGVTPNMIVGTATE VIAAEGKIVTAGGIDTHVHFINPDQVDVALANGITTLFGG GTGPAEGSKATTVTPGPWNIEKMLKSTEGLPINVGILGKG HGSSIAPIMEQIDAGAAGLXIHEDWGATPASIDRSLTVAD EADVQVAIHSDTLNEAGFLEDTLRAINGRVIHSFHVEGAG GGHAPDIMAMAGHPNVLPSSTNPTRPFTVNTIDEHLDMLM VCHHLKQNIPEDVAFADSRIRPETIAAEDILHDLGIISMM STDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDN FRAKRYVSKYTINPAIAQGIAHEVGSIEEGKFADLVLWEP KFFGVKADRVIKGGIIAYAQIGDPSASIPTPQPVMGRRMY GTVGDLIHDTNITFMSKSSIQQGVPAKLGLKRRIGTVKNC RNIGKKDMKWNDVTTDIDINPETYEVKVDGEVLTCEPVKE LPMAQRYFLF Description Functional site 1) chain C residue 309 type sequence V description binding site for residue EDO A 201 source : AC1 2) chain C residue 310 type sequence N description binding site for residue EDO A 201 source : AC1 3) chain C residue 559 type sequence K description binding site for residue EDO A 201 source : AC1 4) chain C residue 568 type sequence F description binding site for residue EDO A 202 source : AC2 5) chain C residue 570 type sequence F description binding site for residue EDO A 202 source : AC2 6) chain B residue 84 type sequence E description binding site for residue EDO A 205 source : AC5 7) chain B residue 101 type sequence D description binding site for residue EDO B 201 source : AC6 8) chain C residue 229 type sequence P description binding site for residue EDO B 201 source : AC6 9) chain B residue 116 type sequence R description binding site for residue SO4 B 202 source : AC7 10) chain C residue 220 type sequence X description binding site for residue NI C 601 source : AC8 11) chain C residue 222 type sequence H description binding site for residue NI C 601 source : AC8 12) chain C residue 249 type sequence H description binding site for residue NI C 601 source : AC8 13) chain C residue 275 type sequence H description binding site for residue NI C 601 source : AC8 14) chain C residue 280 type sequence G description binding site for residue NI C 601 source : AC8 15) chain C residue 137 type sequence H description binding site for residue NI C 602 source : AC9 16) chain C residue 139 type sequence H description binding site for residue NI C 602 source : AC9 17) chain C residue 220 type sequence X description binding site for residue NI C 602 source : AC9 18) chain C residue 363 type sequence D description binding site for residue NI C 602 source : AC9 19) chain C residue 34 type sequence D description binding site for residue EDO C 603 source : AD1 20) chain C residue 36 type sequence T description binding site for residue EDO C 603 source : AD1 21) chain C residue 38 type sequence Y description binding site for residue EDO C 603 source : AD1 22) chain B residue 70 type sequence P description binding site for residue EDO C 604 source : AD2 23) chain B residue 73 type sequence T description binding site for residue EDO C 604 source : AD2 24) chain C residue 7 type sequence Q description binding site for residue EDO C 604 source : AD2 25) chain C residue 11 type sequence S description binding site for residue EDO C 604 source : AD2 26) chain C residue 286 type sequence D description binding site for residue EDO C 605 source : AD3 27) chain C residue 289 type sequence A description binding site for residue EDO C 605 source : AD3 28) chain C residue 537 type sequence I description binding site for residue EDO C 605 source : AD3 29) chain C residue 539 type sequence I description binding site for residue EDO C 605 source : AD3 30) chain C residue 93 type sequence Y description binding site for residue EDO C 606 source : AD4 31) chain C residue 423 type sequence E description binding site for residue EDO C 606 source : AD4 32) chain C residue 501 type sequence Q description binding site for residue EDO C 606 source : AD4 33) chain C residue 513 type sequence R description binding site for residue EDO C 606 source : AD4 34) chain C residue 514 type sequence I description binding site for residue EDO C 606 source : AD4 35) chain C residue 33 type sequence K description binding site for residue EDO C 607 source : AD5 36) chain C residue 35 type sequence Y description binding site for residue EDO C 607 source : AD5 37) chain C residue 536 type sequence D description binding site for residue EDO C 608 source : AD6 38) chain C residue 538 type sequence D description binding site for residue EDO C 608 source : AD6 39) chain C residue 547 type sequence K description binding site for residue EDO C 608 source : AD6 40) chain C residue 549 type sequence D description binding site for residue EDO C 608 source : AD6 41) chain C residue 550 type sequence G description binding site for residue EDO C 608 source : AD6 42) chain B residue 39 type sequence P description binding site for residue EDO C 609 source : AD7 43) chain B residue 76 type sequence R description binding site for residue EDO C 609 source : AD7 44) chain B residue 78 type sequence E description binding site for residue EDO C 609 source : AD7 45) chain C residue 337 type sequence D description binding site for residue EDO C 609 source : AD7 46) chain C residue 338 type sequence S description binding site for residue EDO C 609 source : AD7 47) chain C residue 544 type sequence Y description binding site for residue EDO C 609 source : AD7 48) chain C residue 35 type sequence Y description binding site for residue EDO C 610 source : AD8 49) chain C residue 83 type sequence Y description binding site for residue EDO C 610 source : AD8 50) chain C residue 97 type sequence I description binding site for residue EDO C 610 source : AD8 51) chain C residue 429 type sequence E description binding site for residue EDO C 610 source : AD8 52) chain C residue 143 type sequence P description binding site for residue EDO C 611 source : AD9 53) chain C residue 189 type sequence G description binding site for residue EDO C 611 source : AD9 54) chain C residue 478 type sequence R description binding site for residue EDO C 611 source : AD9 55) chain C residue 309 type sequence V description binding site for residue EDO C 612 source : AE1 56) chain C residue 557 type sequence P description binding site for residue EDO C 612 source : AE1 57) chain C residue 34 type sequence D description binding site for residue EDO C 613 source : AE2 58) chain C residue 35 type sequence Y description binding site for residue EDO C 613 source : AE2 59) chain C residue 317 type sequence D description binding site for residue EDO C 614 source : AE3 60) chain C residue 327 type sequence Q description binding site for residue EDO C 614 source : AE3 61) chain C residue 65 type sequence N description binding site for residue SO4 C 615 source : AE4 62) chain C residue 204 type sequence S description binding site for residue SO4 C 615 source : AE4 63) chain C residue 205 type sequence I description binding site for residue SO4 C 615 source : AE4 64) chain C residue 558 type sequence V description binding site for residue SO4 C 616 source : AE5 65) chain C residue 559 type sequence K description binding site for residue SO4 C 616 source : AE5 66) chain C residue 560 type sequence E description binding site for residue SO4 C 616 source : AE5 67) chain C residue 137 type sequence H description binding site for residue 2PA C 617 source : AE6 68) chain C residue 139 type sequence H description binding site for residue 2PA C 617 source : AE6 69) chain C residue 170 type sequence A description binding site for residue 2PA C 617 source : AE6 70) chain C residue 220 type sequence X description binding site for residue 2PA C 617 source : AE6 71) chain C residue 222 type sequence H description binding site for residue 2PA C 617 source : AE6 72) chain C residue 249 type sequence H description binding site for residue 2PA C 617 source : AE6 73) chain C residue 275 type sequence H description binding site for residue 2PA C 617 source : AE6 74) chain C residue 280 type sequence G description binding site for residue 2PA C 617 source : AE6 75) chain C residue 323 type sequence H description binding site for residue 2PA C 617 source : AE6 76) chain C residue 363 type sequence D description binding site for residue 2PA C 617 source : AE6 77) chain C residue 366 type sequence A description binding site for residue 2PA C 617 source : AE6 78) chain C residue 367 type sequence M description binding site for residue 2PA C 617 source : AE6 79) chain B residue 71 type sequence S description binding site for residue SO4 C 618 source : AE7 80) chain B residue 72 type sequence G description binding site for residue SO4 C 618 source : AE7 81) chain C residue 11 type sequence S description binding site for residue SO4 C 618 source : AE7 82) chain C residue 12 type sequence Y description binding site for residue SO4 C 618 source : AE7 83) chain C residue 43 type sequence N description binding site for residue SO4 C 618 source : AE7 84) chain C residue 48 type sequence K description binding site for residue SO4 C 618 source : AE7 85) chain C residue 326 type sequence K description binding site for residue SO4 C 618 source : AE7 86) chain C residue 329 type sequence I description binding site for residue SO4 C 618 source : AE7 87) chain C residue 511 type sequence K description binding site for residue SO4 C 619 source : AE8 88) chain C residue 511 type sequence K description binding site for residue SO4 C 619 source : AE8 89) chain C residue 511 type sequence K description binding site for residue SO4 C 619 source : AE8 90) chain C residue 518 type sequence K description binding site for residue SO4 C 620 source : AE9 91) chain C residue 518 type sequence K description binding site for residue SO4 C 620 source : AE9 92) chain C residue 320-336 type prosite sequence MVCHHLKQNIPEDVAFA description UREASE_2 Urease active site. MVCHHLkqnIpeDVaFA source prosite : PS00145 93) chain C residue 130-143 type prosite sequence TAGGIDTHVHFINP description UREASE_1 Urease nickel ligands signature. TAGGIDtHVHfinP source prosite : PS01120 94) chain C residue 363 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231 source Swiss-Prot : SWS_FT_FI2 95) chain C residue 137 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231 source Swiss-Prot : SWS_FT_FI2 96) chain C residue 275 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231 source Swiss-Prot : SWS_FT_FI2 97) chain C residue 170 type BINDING sequence A description BINDING => ECO:0000269|PubMed:30969470 source Swiss-Prot : SWS_FT_FI3 98) chain C residue 222 type BINDING sequence H description BINDING => ECO:0000269|PubMed:30969470 source Swiss-Prot : SWS_FT_FI3 99) chain C residue 249 type BINDING sequence H description BINDING => ECO:0000269|PubMed:30969470 source Swiss-Prot : SWS_FT_FI3 100) chain C residue 366 type BINDING sequence A description BINDING => ECO:0000269|PubMed:30969470 source Swiss-Prot : SWS_FT_FI3 101) chain C residue 139 type BINDING sequence H description BINDING => ECO:0000269|PubMed:30969470 source Swiss-Prot : SWS_FT_FI3 102) chain C residue 220 type BINDING sequence X description via carbamate group => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231 source Swiss-Prot : SWS_FT_FI4 103) chain C residue 220 type MOD_RES sequence X description N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231, ECO:0007744|PDB:1IE7, ECO:0007744|PDB:1S3T, ECO:0007744|PDB:1UBP, ECO:0007744|PDB:2UBP, ECO:0007744|PDB:4UBP source Swiss-Prot : SWS_FT_FI5 104) chain C residue 323 type ACT_SITE sequence H description Proton donor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1

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