eF-site ID 1bll-E PDB Code 1bll Chain E click to enlarge Title X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE Classification HYDROLASE/HYDROLASE INHIBITOR Compound LEUCINE AMINOPEPTIDASE Source null (1BLL) Sequence E:  TKGLVLGIYSKEDEPQFTSAGENFNKLVSGKLREILNISG PPLKAGKTRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWH EGKENIRAAVAAGCRQIQDLEIPSVEVDPCGDAQAAAEGA VLGLYEYDDLKQKRKVVVSAKLHGSEDQEAWQRGVLFASG QNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDVFIR PKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEP PLVFVGKGITFDSGGISIKAAANMDLMRADMGGAATICSA IVSAAKLDLPINIVGLAPLCENMPSGKANKPGDVVRARNG KTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGA MDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLF EHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHP KWAHLDIAGVMTNKDEVPYLRKGMAGRPTRTLIEFLFRFS Q Description Functional site 1) chain E residue 255 type sequence D description BINDING SITE FOR RESIDUE ZN E 488 source : AC1 2) chain E residue 332 type sequence D description BINDING SITE FOR RESIDUE ZN E 488 source : AC1 3) chain E residue 334 type sequence E description BINDING SITE FOR RESIDUE ZN E 488 source : AC1 4) chain E residue 250 type sequence K description BINDING SITE FOR RESIDUE ZN E 489 source : AC2 5) chain E residue 255 type sequence D description BINDING SITE FOR RESIDUE ZN E 489 source : AC2 6) chain E residue 273 type sequence D description BINDING SITE FOR RESIDUE ZN E 489 source : AC2 7) chain E residue 334 type sequence E description BINDING SITE FOR RESIDUE ZN E 489 source : AC2 8) chain E residue 250 type sequence K description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 9) chain E residue 255 type sequence D description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 10) chain E residue 262 type sequence K description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 11) chain E residue 270 type sequence M description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 12) chain E residue 273 type sequence D description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 13) chain E residue 332 type sequence D description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 14) chain E residue 334 type sequence E description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 15) chain E residue 336 type sequence R description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 16) chain E residue 359 type sequence T description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 17) chain E residue 360 type sequence L description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 18) chain E residue 362 type sequence G description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 19) chain E residue 363 type sequence A description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 20) chain E residue 366 type sequence I description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 21) chain E residue 366 type sequence I description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 22) chain E residue 425 type sequence R description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 23) chain E residue 428 type sequence G description BINDING SITE FOR CHAIN I OF AMASTATIN source : AC3 24) chain E residue 294 type catalytic sequence I description 587 source MCSA : MCSA1 25) chain E residue 368 type catalytic sequence L description 587 source MCSA : MCSA1 26) chain E residue 45 type MOD_RES sequence P description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPY7 source Swiss-Prot : SWS_FT_FI9 27) chain E residue 61 type MOD_RES sequence F description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPY7 source Swiss-Prot : SWS_FT_FI9 28) chain E residue 103 type MOD_RES sequence L description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPY7 source Swiss-Prot : SWS_FT_FI9 29) chain E residue 476 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPY7 source Swiss-Prot : SWS_FT_FI9 30) chain E residue 180 type MOD_RES sequence P description Phosphoserine => ECO:0000250|UniProtKB:Q9CPY7 source Swiss-Prot : SWS_FT_FI10 31) chain E residue 194 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P28838 source Swiss-Prot : SWS_FT_FI11 32) chain E residue 238 type MOD_RES sequence P description Phosphoserine => ECO:0000250|UniProtKB:P28838 source Swiss-Prot : SWS_FT_FI11 33) chain E residue 455 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPY7 source Swiss-Prot : SWS_FT_FI12 34) chain E residue 294 type ACT_SITE sequence I description ACT_SITE => ECO:0000269|PubMed:7578088 source Swiss-Prot : SWS_FT_FI1 35) chain E residue 368 type ACT_SITE sequence L description ACT_SITE => ECO:0000269|PubMed:7578088 source Swiss-Prot : SWS_FT_FI1 36) chain E residue 202 type BINDING sequence I description BINDING => ECO:0000305|PubMed:7619821, ECO:0007744|PDB:1LCP source Swiss-Prot : SWS_FT_FI2 37) chain E residue 203 type BINDING sequence R description BINDING => ECO:0000305|PubMed:7619821, ECO:0007744|PDB:1LCP source Swiss-Prot : SWS_FT_FI2 38) chain E residue 205 type BINDING sequence K description BINDING => ECO:0000305|PubMed:7619821, ECO:0007744|PDB:1LCP source Swiss-Prot : SWS_FT_FI2 39) chain E residue 303 type BINDING sequence C description BINDING => ECO:0000305|PubMed:7619821, ECO:0007744|PDB:1LCP source Swiss-Prot : SWS_FT_FI2 40) chain E residue 282 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A source Swiss-Prot : SWS_FT_FI3 41) chain E residue 287 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A source Swiss-Prot : SWS_FT_FI3 42) chain E residue 305 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A source Swiss-Prot : SWS_FT_FI3 43) chain E residue 292 type BINDING sequence L description BINDING => ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LCP source Swiss-Prot : SWS_FT_FI4 44) chain E residue 294 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7578088, ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LAN, ECO:0007744|PDB:1LCP source Swiss-Prot : SWS_FT_FI5 45) chain E residue 364 type BINDING sequence M description BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A source Swiss-Prot : SWS_FT_FI6 46) chain E residue 42 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q68FS4 source Swiss-Prot : SWS_FT_FI8 47) chain E residue 54 type MOD_RES sequence F description Phosphoserine => ECO:0000250|UniProtKB:Q68FS4 source Swiss-Prot : SWS_FT_FI8 48) chain E residue 330-337 type prosite sequence NTDAEGRL description CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL source prosite : PS00631 49) chain E residue 366 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345, ECO:0007744|PDB:1BPM, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A source Swiss-Prot : SWS_FT_FI7

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