eF-site ID 3fjx-A PDB Code 3fjx Chain A click to enlarge Title E. coli EPSP synthase (T97I) liganded with S3P Classification TRANSFERASE Compound 3-phosphoshikimate 1-carboxyvinyltransferase Source null (AROA_ECOLI) Sequence A:  MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTV LTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGG PLHAEGALELFLGNAGIAMRPLAAALCLGSNDIVLTGEPR 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 22 type sequence K description BINDING SITE FOR RESIDUE FMT A 429 source : AC2 14) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE FMT A 429 source : AC2 15) chain A residue 341 type sequence E description BINDING SITE FOR RESIDUE FMT A 429 source : AC2 16) chain A residue 344 type sequence R description BINDING SITE FOR RESIDUE FMT A 429 source : AC2 17) chain A residue 385 type sequence H description BINDING SITE FOR RESIDUE FMT A 429 source : AC2 18) chain A residue 386 type sequence R description BINDING SITE FOR RESIDUE FMT A 429 source : AC2 19) chain A residue 380 type sequence A description BINDING SITE FOR RESIDUE FMT A 430 source : AC3 20) chain A residue 382 type sequence Y 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 22 type sequence K description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 26) chain A residue 94 type sequence N description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 27) chain A residue 96 type sequence G description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 28) chain A residue 97 type sequence I description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 29) chain A residue 124 type sequence R description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 30) chain A residue 341 type sequence E description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 31) chain A residue 411 type sequence K description BINDING SITE FOR RESIDUE FMT A 432 source : AC5 32) chain A residue 335 type sequence Y description BINDING SITE FOR RESIDUE FMT A 433 source : AC6 33) chain A residue 339 type sequence V description BINDING SITE FOR RESIDUE FMT A 433 source : AC6 34) chain A residue 58 type sequence T description BINDING SITE FOR RESIDUE FMT A 434 source : AC7 35) chain A residue 62 type sequence V description BINDING SITE FOR RESIDUE FMT A 434 source : AC7 36) chain A residue 63 type sequence S description BINDING SITE FOR RESIDUE FMT A 434 source : AC7 37) chain A residue 64 type sequence Y description BINDING SITE FOR RESIDUE FMT A 434 source : AC7 38) chain A residue 65 type sequence T description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 39) chain A residue 66 type sequence L description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 40) chain A residue 67 type sequence S description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 41) chain A residue 72 type sequence R description BINDING SITE FOR RESIDUE FMT A 435 source : AC8 42) chain A residue 298 type sequence R description BINDING SITE FOR RESIDUE FMT A 436 source : AC9 43) chain A residue 300 type sequence E description BINDING SITE FOR RESIDUE FMT A 436 source : AC9 44) chain A residue 301 type sequence L description BINDING SITE FOR RESIDUE FMT A 436 source : AC9 45) chain A residue 324 type sequence F description BINDING SITE FOR RESIDUE FMT A 436 source : AC9 46) chain A residue 90-104 type prosite sequence LFLGNAGIAMRPLAA description EPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGIAMRpLaA source prosite : PS00104 47) chain A residue 338-356 type prosite sequence RVKETDRLFAMATELRKVG description EPSP_SYNTHASE_2 EPSP synthase signature 2. RvKETDRLfAMateLrkVG source prosite : PS00885 48) chain A residue 408 type SITE sequence C description Modified by bromopyruvate => ECO:0000269|PubMed:11171958 source Swiss-Prot : SWS_FT_FI6 49) chain A residue 411 type SITE sequence K description Modified by bromopyruvate => ECO:0000269|PubMed:11171958 source Swiss-Prot : SWS_FT_FI6 50) chain A residue 313 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 341 type ACT_SITE sequence E description Proton donor => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:15736934, ECO:0000305|PubMed:11171958 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 169 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI3 54) chain A residue 340 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI3 55) chain A residue 27 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 197 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI4 57) chain A residue 336 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI4 58) chain A residue 124 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 344 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI5 60) chain A residue 386 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI5 61) chain A residue 411 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556 source Swiss-Prot : SWS_FT_FI5 62) chain A residue 49 type catalytic sequence D description 457 source MCSA : MCSA1 63) chain A residue 94 type catalytic sequence N description 457 source MCSA : MCSA1 64) chain A residue 313 type catalytic sequence D description 457 source MCSA : MCSA1 65) chain A residue 341 type catalytic sequence E description 457 source MCSA : MCSA1 66) chain A residue 385 type catalytic sequence H description 457 source MCSA : MCSA1 67) chain A residue 386 type catalytic sequence R description 457 source MCSA : MCSA1 68) chain A residue 411 type catalytic sequence K description 457 source MCSA : MCSA1

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