eF-site ID 1nlu-A PDB Code 1nlu Chain A click to enlarge Title Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin Classification HYDROLASE/HYDROLASE INHIBITOR Compound SEDOLISIN Source Pseudomonas sp. (strain 101) (Achromobacter parvulus T1) (1NLU) Sequence A:  GTAKGHNPTEFPTIYDASSAPTAANTTVGIITIGGVSQTL QDLQQFTSANGLASVNTQTIQTGSSNGDYSDDQQGQGEWD LDSQSIVGSAGGAVQQLLFYMADQSASGNTGLTQAFNQAV SDNVAKVINVSLGWCEADANADGTLQAEDRIFATAAAQGQ TFSVSSGDEGVYECNNRGYPDGSTYSVSWPASSPNVIAVG GTTLYTTSAGAYSNETVWNEGLDSNGKLWATGGGYSVYES KPSWQSVVSGTPGRRLLPDISFDAAQGTGALIYNYGQLQQ IGGTSLASPIFVGLWARLQSANSNSLGFPAASFYSAISST PSLVHDVKSGNNGYGGYGYNAGTGWDYPTGWGSLDIAKLS AYIRSNGF Description (1)  SERINE-CARBOXYL PROTEINASE (E.C.3.4.21.100) Functional site 1) chain A residue 328 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC1 2) chain A residue 329 type sequence V description BINDING SITE FOR RESIDUE CA A 501 source : AC1 3) chain A residue 344 type sequence G description BINDING SITE FOR RESIDUE CA A 501 source : AC1 4) chain A residue 346 type sequence G description BINDING SITE FOR RESIDUE CA A 501 source : AC1 5) chain A residue 348 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC1 6) chain A residue 74 type sequence D description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 7) chain A residue 80 type sequence E description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 8) chain A residue 81 type sequence W description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 9) chain A residue 133 type sequence S description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 10) chain A residue 134 type sequence L description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 11) chain A residue 135 type sequence G description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 12) chain A residue 136 type sequence W description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 13) chain A residue 169 type sequence G description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 14) chain A residue 170 type sequence D description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 15) chain A residue 171 type sequence E description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 16) chain A residue 175 type sequence E description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 17) chain A residue 179 type sequence R description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 18) chain A residue 190 type sequence S description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 19) chain A residue 285 type sequence G description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 20) chain A residue 286 type sequence T description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 21) chain A residue 287 type sequence S description BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN source : AC2 22) chain A residue 79 type sequence G description BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN source : AC3 23) chain A residue 80 type sequence E description BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN source : AC3 24) chain A residue 222 type sequence E description BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN source : AC3 25) chain A residue 231 type sequence W description BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN source : AC3 26) chain A residue 268 type sequence Q description BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN source : AC3 27) chain A residue 281 type sequence Q description BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN source : AC3 28) chain A residue 283 type sequence I description BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN source : AC3 29) chain A residue 284 type sequence G description BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN source : AC3 30) chain A residue 80 type catalytic sequence E description 380 source MCSA : MCSA1 31) chain A residue 84 type catalytic sequence D description 380 source MCSA : MCSA1 32) chain A residue 170 type catalytic sequence D description 380 source MCSA : MCSA1 33) chain A residue 287 type catalytic sequence S description 380 source MCSA : MCSA1 34) chain A residue 328 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 35) chain A residue 329 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 36) chain A residue 344 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 37) chain A residue 346 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 348 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 80 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:10488127 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 84 type ACT_SITE sequence D description Charge relay system => ECO:0000269|PubMed:10488127 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 287 type ACT_SITE sequence S description Charge relay system => ECO:0000269|PubMed:10488127 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 285-295 type prosite sequence GTSLASPIFVG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSlAsPiFVG source prosite : PS00138

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