eF-site ID 1gwu-A PDB Code 1gwu Chain A click to enlarge Title RECOMBINANT HORSERADISH PEROXIDASE C1A ALA140GLY Classification OXIDOREDUCTASE Compound PEROXIDASE C1A Source Armoracia rusticana (Horseradish) (Armoracia laphatifolia) (PERA_ARMRU) Sequence A:  MQLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRL HFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPV IDRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRV PLGRRDSLQAFLDLANANLPGPFFTLPQLKDSFRNVGLNR SSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNT TYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEE QKGLIQSDQELFSSPNATDTIPLVRSFANSTQTFFNAFVE AMDRMGNITPLTGTQGQIRLNCRVVNS Description Functional site 1) chain A residue 43 type sequence D description BINDING SITE FOR RESIDUE CA A1307 source : AC2 2) chain A residue 46 type sequence V description BINDING SITE FOR RESIDUE CA A1307 source : AC2 3) chain A residue 48 type sequence G description BINDING SITE FOR RESIDUE CA A1307 source : AC2 4) chain A residue 50 type sequence D description BINDING SITE FOR RESIDUE CA A1307 source : AC2 5) chain A residue 52 type sequence S description BINDING SITE FOR RESIDUE CA A1307 source : AC2 6) chain A residue 171 type sequence T description BINDING SITE FOR RESIDUE CA A1308 source : AC3 7) chain A residue 222 type sequence D description BINDING SITE FOR RESIDUE CA A1308 source : AC3 8) chain A residue 225 type sequence T description BINDING SITE FOR RESIDUE CA A1308 source : AC3 9) chain A residue 228 type sequence I description BINDING SITE FOR RESIDUE CA A1308 source : AC3 10) chain A residue 230 type sequence D description BINDING SITE FOR RESIDUE CA A1308 source : AC3 11) chain A residue 38 type sequence R description BINDING SITE FOR RESIDUE ACT A1309 source : AC4 12) chain A residue 41 type sequence F description BINDING SITE FOR RESIDUE ACT A1309 source : AC4 13) chain A residue 42 type sequence H description BINDING SITE FOR RESIDUE ACT A1309 source : AC4 14) chain A residue 139 type sequence P description BINDING SITE FOR RESIDUE ACT A1309 source : AC4 15) chain A residue 65 type sequence K description BINDING SITE FOR RESIDUE ACT A1310 source : AC5 16) chain A residue 77 type sequence F description BINDING SITE FOR RESIDUE ACT A1310 source : AC5 17) chain A residue 302 type sequence R description BINDING SITE FOR RESIDUE ACT A1310 source : AC5 18) chain A residue 31 type sequence R description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 19) chain A residue 34 type sequence A description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 20) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 21) chain A residue 38 type sequence R description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 22) chain A residue 41 type sequence F description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 23) chain A residue 73 type sequence S description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 24) chain A residue 75 type sequence R description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 25) chain A residue 139 type sequence P description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 26) chain A residue 140 type sequence G description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 27) chain A residue 141 type sequence P description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 28) chain A residue 152 type sequence F description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 29) chain A residue 166 type sequence L description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 30) chain A residue 167 type sequence S description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 31) chain A residue 169 type sequence G description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 32) chain A residue 170 type sequence H description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 33) chain A residue 172 type sequence F description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 34) chain A residue 173 type sequence G description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 35) chain A residue 174 type sequence K description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 36) chain A residue 175 type sequence N description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 37) chain A residue 176 type sequence Q description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 38) chain A residue 179 type sequence F description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 39) chain A residue 221 type sequence F description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 40) chain A residue 246 type sequence S description BINDING SITE FOR RESIDUE HEM A1306 source : AC6 41) chain A residue 38 type catalytic sequence R description 239 source MCSA : MCSA1 42) chain A residue 42 type catalytic sequence H description 239 source MCSA : MCSA1 43) chain A residue 70 type catalytic sequence N description 239 source MCSA : MCSA1 44) chain A residue 170 type catalytic sequence H description 239 source MCSA : MCSA1 45) chain A residue 43 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 46) chain A residue 225 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 47) chain A residue 230 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 48) chain A residue 46 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 49) chain A residue 48 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 50) chain A residue 50 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 51) chain A residue 52 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 52) chain A residue 64 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 53) chain A residue 139 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI2 54) chain A residue 171 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 55) chain A residue 222 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 56) chain A residue 170 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI3 57) chain A residue 38 type SITE sequence R description Transition state stabilizer source Swiss-Prot : SWS_FT_FI4 58) chain A residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:1001465 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 158 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI7 60) chain A residue 186 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI7 61) chain A residue 198 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI7 62) chain A residue 214 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI7 63) chain A residue 255 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI7 64) chain A residue 268 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI7 65) chain A residue 42 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 66) chain A residue 13 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1001465 source Swiss-Prot : SWS_FT_FI6 67) chain A residue 57 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1001465 source Swiss-Prot : SWS_FT_FI6 68) chain A residue 162-172 type prosite sequence DLVALSGGHTF description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DLVALSGGHTF source prosite : PS00435 69) chain A residue 33-44 type prosite sequence AASILRLHFHDC description PEROXIDASE_2 Peroxidases active site signature. AAsiLRLhFHDC source prosite : PS00436

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