eF-site ID 1j1z-B PDB Code 1j1z Chain B click to enlarge Title Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with substrate Classification LIGASE Compound Argininosuccinate Synthetase Source null (ASSY_THET8) Sequence B:  MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEE VEEAREKALRTGASKAIALDLKEEFVRDFVFPMMRAGAVY EGYYLLGTSIARPLIAKHLVRIAEEEGAEAIAHGATGKGN DQVRFELTAYALKPDIKVIAPWREWSFQGRKEMIAYAEAH GIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEI GGRHGVGRVDIVENRFVGMKSRGVYETPGGTILYHARRAV ESLTLDREVLHQRDMLSPKYAELVYYGFWYAPEREALQAY FDHVARSVTGVARLKLYKGNVYVVGRKAPKSLYRQDLVSF GYDQKDAEGFIKIQALRLRVRALVER Description Functional site 1) chain B residue 6 type sequence A description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 2) chain B residue 7 type sequence Y description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 3) chain B residue 8 type sequence S description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 4) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 5) chain B residue 12 type sequence D description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 6) chain B residue 13 type sequence T description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 7) chain B residue 31 type sequence F description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 8) chain B residue 32 type sequence T description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 9) chain B residue 33 type sequence A description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 10) chain B residue 37 type sequence Q description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 11) chain B residue 92 type sequence R description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 12) chain B residue 113 type sequence H description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 13) chain B residue 114 type sequence G description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 14) chain B residue 125 type sequence F description BINDING SITE FOR RESIDUE ATP B 2510 source : AC2 15) chain B residue 84 type sequence Y description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 16) chain B residue 88 type sequence T description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 17) chain B residue 89 type sequence S description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 18) chain B residue 120 type sequence N description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 19) chain B residue 124 type sequence R description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 20) chain B residue 173 type sequence S description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 21) chain B residue 174 type sequence M description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 22) chain B residue 175 type sequence D description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 23) chain B residue 182 type sequence S description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 24) chain B residue 184 type sequence E description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 25) chain B residue 258 type sequence E description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 26) chain B residue 270 type sequence Y description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 27) chain B residue 310 type sequence Y description BINDING SITE FOR RESIDUE CIR B 2520 source : AC6 28) chain B residue 115 type sequence A description BINDING SITE FOR RESIDUE ASP A 2530 source : BC1 29) chain B residue 116 type sequence T description BINDING SITE FOR RESIDUE ASP A 2530 source : BC1 30) chain B residue 119 type sequence G description BINDING SITE FOR RESIDUE ASP A 2530 source : BC1 31) chain B residue 120 type sequence N description BINDING SITE FOR RESIDUE ASP A 2530 source : BC1 32) chain B residue 121 type sequence D description BINDING SITE FOR RESIDUE ASP A 2530 source : BC1 33) chain B residue 12 type catalytic sequence D description 316 source MCSA : MCSA2 34) chain B residue 92 type catalytic sequence R description 316 source MCSA : MCSA2 35) chain B residue 121 type catalytic sequence D description 316 source MCSA : MCSA2 36) chain B residue 173 type catalytic sequence S description 316 source MCSA : MCSA2 37) chain B residue 6 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 33 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 114 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 84 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 41) chain B residue 89 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 42) chain B residue 116 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 43) chain B residue 120 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 44) chain B residue 121 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 45) chain B residue 124 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 46) chain B residue 173 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 47) chain B residue 182 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 48) chain B residue 258 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 49) chain B residue 270 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2

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