eF-site ID 2wxb-AB PDB Code 2wxb Chain A, B click to enlarge Title Acetylglutamate kinase from Escherichia coli free of substrates Classification TRANSFERASE Compound ACETYLGLUTAMATE KINASE Source (ARGB_ECOLI) Sequence A:  MNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIV HGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALA GTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELGH VGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNA DQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAKA EQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAE QLPALFNGMPMGTRILA B:  MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVI VHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGAL AGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELG HVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVN ADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAK AEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHA EQLPALFNGMPMGTRILA Description Functional site 1) chain A residue 8 type sequence K description BINDING SITE FOR RESIDUE DTU A 1259 source : AC1 2) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE DTU A 1259 source : AC1 3) chain A residue 12 type sequence V description BINDING SITE FOR RESIDUE DTU A 1259 source : AC1 4) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE DTU A 1259 source : AC1 5) chain A residue 160 type sequence N description BINDING SITE FOR RESIDUE ACT A 1260 source : AC2 6) chain B residue 8 type sequence K description BINDING SITE FOR RESIDUE DTU B 1259 source : AC3 7) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE DTU B 1259 source : AC3 8) chain B residue 11 type sequence G description BINDING SITE FOR RESIDUE DTU B 1259 source : AC3 9) chain B residue 45 type sequence G description BINDING SITE FOR RESIDUE DTU B 1259 source : AC3 10) chain B residue 180 type sequence S description BINDING SITE FOR RESIDUE DTU B 1259 source : AC3 11) chain A residue 135 type sequence S description BINDING SITE FOR RESIDUE EDO B 1260 source : AC4 12) chain A residue 136 type sequence L description BINDING SITE FOR RESIDUE EDO B 1260 source : AC4 13) chain A residue 139 type sequence N description BINDING SITE FOR RESIDUE EDO B 1260 source : AC4 14) chain B residue 135 type sequence S description BINDING SITE FOR RESIDUE EDO B 1260 source : AC4 15) chain B residue 139 type sequence N description BINDING SITE FOR RESIDUE EDO B 1260 source : AC4 16) chain A residue 8 type catalytic sequence K description 870 source MCSA : MCSA1 17) chain A residue 11 type catalytic sequence G description 870 source MCSA : MCSA1 18) chain A residue 45 type catalytic sequence G description 870 source MCSA : MCSA1 19) chain A residue 162 type catalytic sequence D description 870 source MCSA : MCSA1 20) chain A residue 217 type catalytic sequence K description 870 source MCSA : MCSA1 21) chain B residue 8 type catalytic sequence K description 870 source MCSA : MCSA2 22) chain B residue 11 type catalytic sequence G description 870 source MCSA : MCSA2 23) chain B residue 45 type catalytic sequence G description 870 source MCSA : MCSA2 24) chain B residue 162 type catalytic sequence D description 870 source MCSA : MCSA2 25) chain B residue 217 type catalytic sequence K description 870 source MCSA : MCSA2 26) chain A residue 44 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 66 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 158 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 44 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 66 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 158 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 181 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 209 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 181 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 209 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12875848 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 8 type SITE sequence K description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305|PubMed:12875848 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 217 type SITE sequence K description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305|PubMed:12875848 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 8 type SITE sequence K description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305|PubMed:12875848 source Swiss-Prot : SWS_FT_FI3 39) chain B residue 217 type SITE sequence K description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305|PubMed:12875848 source Swiss-Prot : SWS_FT_FI3

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