eF-site ID 3fk0-A PDB Code 3fk0 Chain A click to enlarge Title E. coli EPSP synthase (TIPS mutation) liganded with S3P Classification TRANSFERASE Compound 3-phosphoshikimate 1-carboxyvinyltransferase Source Escherichia coli (strain K12) (AROA_ECOLI) Sequence A:  MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTV LTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGG PLHAEGALELFLGNAGIAMRSLAAALCLGSNDIVLTGEPR MKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGG NVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPY IDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVE GDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVL EKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIAT AALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVE EGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTP VTILDPKCTAKTFPDYFEQLARISQAA Description Functional site 1) chain A residue 22 type sequence K description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 2) chain A residue 23 type sequence S description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 3) chain A residue 27 type sequence R description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 4) chain A residue 97 type sequence I description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 5) chain A residue 169 type sequence S description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 6) chain A residue 170 type sequence S description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 7) chain A residue 171 type sequence Q description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 8) chain A residue 197 type sequence S description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 9) chain A residue 200 type sequence Y description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 10) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 11) chain A residue 336 type sequence N description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 12) chain A residue 340 type sequence K description BINDING SITE FOR RESIDUE S3P A 428 source : AC1 13) chain A residue 380 type sequence A description BINDING SITE FOR RESIDUE FMT A 429 source : AC2 14) chain A residue 382 type sequence Y description BINDING SITE FOR RESIDUE FMT A 429 source : AC2 15) chain A residue 22 type sequence K description BINDING SITE FOR RESIDUE FMT A 430 source : AC3 16) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE FMT A 430 source : AC3 17) chain A residue 341 type sequence E description BINDING SITE FOR RESIDUE FMT A 430 source : AC3 18) chain A residue 344 type sequence R description BINDING SITE FOR RESIDUE FMT A 430 source : AC3 19) chain A residue 385 type sequence H description BINDING SITE FOR RESIDUE FMT A 430 source : AC3 20) chain A residue 386 type sequence R description BINDING SITE FOR RESIDUE FMT A 430 source : AC3 21) chain A residue 373 type sequence K description BINDING SITE FOR RESIDUE FMT A 431 source : AC4 22) chain A residue 374 type sequence L description BINDING SITE FOR RESIDUE FMT A 431 source : AC4 23) chain A residue 397 type sequence S description BINDING SITE FOR RESIDUE FMT A 431 source : AC4 24) chain A residue 398 type sequence D description BINDING SITE FOR RESIDUE FMT A 431 source : AC4 25) chain A residue 65 type sequence T description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 26) chain A residue 66 type sequence L description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 27) chain A residue 67 type sequence S description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 28) chain A residue 72 type sequence R description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 29) chain A residue 298 type sequence R description BINDING SITE FOR RESIDUE FMT A 433 source : AC6 30) chain A residue 300 type sequence E description BINDING SITE FOR RESIDUE FMT A 433 source : AC6 31) chain A residue 301 type sequence L description BINDING SITE FOR RESIDUE FMT A 433 source : AC6 32) chain A residue 324 type sequence F description BINDING SITE FOR RESIDUE FMT A 433 source : AC6 33) chain A residue 58 type sequence T description BINDING SITE FOR RESIDUE FMT A 434 source : AC7 34) chain A residue 62 type sequence V description BINDING SITE FOR RESIDUE FMT A 434 source : AC7 35) chain A residue 63 type sequence S description BINDING SITE FOR RESIDUE FMT A 434 source : AC7 36) chain A residue 64 type sequence Y description BINDING SITE FOR RESIDUE FMT A 434 source : AC7 37) chain A residue 5 type sequence T description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 38) chain A residue 143 type sequence L description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 39) chain A residue 152 type sequence R description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 40) chain A residue 376 type sequence F description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 41) chain A residue 402 type sequence T description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 42) chain A residue 38 type sequence K description BINDING SITE FOR RESIDUE FMT A 437 source : BC1 43) chain A residue 363 type sequence H description BINDING SITE FOR RESIDUE FMT A 437 source : BC1 44) chain A residue 49 type catalytic sequence D description 457 source MCSA : MCSA1 45) chain A residue 94 type catalytic sequence N description 457 source MCSA : MCSA1 46) chain A residue 313 type catalytic sequence D description 457 source MCSA : MCSA1 47) chain A residue 341 type catalytic sequence E description 457 source MCSA : MCSA1 48) chain A residue 385 type catalytic sequence H description 457 source MCSA : MCSA1 49) chain A residue 386 type catalytic sequence R description 457 source MCSA : MCSA1 50) chain A residue 411 type catalytic sequence K description 457 source MCSA : MCSA1 51) chain A residue 90-104 type prosite sequence LFLGNAGIAMRSLAA description EPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGIAMRsLaA source prosite : PS00104 52) chain A residue 338-356 type prosite sequence RVKETDRLFAMATELRKVG description EPSP_SYNTHASE_2 EPSP synthase signature 2. RvKETDRLfAMateLrkVG source prosite : PS00885 53) chain A residue 313 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:13129913 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00210 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 96 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00210 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 124 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00210 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 171 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00210 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 344 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00210 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 386 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00210 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 411 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00210 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 23 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S source Swiss-Prot : SWS_FT_FI3 62) chain A residue 27 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S source Swiss-Prot : SWS_FT_FI3 63) chain A residue 169 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S source Swiss-Prot : SWS_FT_FI3 64) chain A residue 170 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S source Swiss-Prot : SWS_FT_FI3 65) chain A residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S source Swiss-Prot : SWS_FT_FI3 66) chain A residue 313 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S source Swiss-Prot : SWS_FT_FI3 67) chain A residue 336 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S source Swiss-Prot : SWS_FT_FI3 68) chain A residue 340 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S source Swiss-Prot : SWS_FT_FI3 69) chain A residue 408 type SITE sequence C description Modified by bromopyruvate => ECO:0000269|PubMed:11171958 source Swiss-Prot : SWS_FT_FI4 70) chain A residue 411 type SITE sequence K description Modified by bromopyruvate => ECO:0000269|PubMed:11171958 source Swiss-Prot : SWS_FT_FI4

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