eF-site ID 2x2w-A PDB Code 2x2w Chain A click to enlarge Title Acetylglutamate kinase from Escherichia coli bound to N-acetyl-L-glutamyl-5-phosphate Classification TRANSFERASE Compound ACETYLGLUTAMATE KINASE Source (ARGB_ECOLI) Sequence A:  MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVI VHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGAL AGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELG HVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVN ADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAK AEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHA EQLPALFNGMPMGTRILA Description Functional site 1) chain A residue 10 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1260 source : AC1 2) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1260 source : AC1 3) chain A residue 12 type sequence V description BINDING SITE FOR RESIDUE SO4 A 1260 source : AC1 4) chain A residue 180 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1260 source : AC1 5) chain A residue 217 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1260 source : AC1 6) chain A residue 8 type sequence K description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 7) chain A residue 9 type sequence L description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 8) chain A residue 10 type sequence G description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 9) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 10) chain A residue 43 type sequence G description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 11) chain A residue 44 type sequence G description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 12) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 13) chain A residue 66 type sequence R description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 14) chain A residue 158 type sequence N description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 15) chain A residue 161 type sequence A description BINDING SITE FOR RESIDUE X2W A 1259 source : AC3 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 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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

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