eF-site ID 2x2w-B PDB Code 2x2w Chain B 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 B:  MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVI VHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGAL AGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELG HVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVN ADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAK AEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHA EQLPALFNGMPMGTRILA Description Functional site 1) chain B residue 11 type sequence G description BINDING SITE FOR RESIDUE SO4 B 1260 source : AC2 2) chain B residue 12 type sequence V description BINDING SITE FOR RESIDUE SO4 B 1260 source : AC2 3) chain B residue 180 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1260 source : AC2 4) chain B residue 181 type sequence D description BINDING SITE FOR RESIDUE SO4 B 1260 source : AC2 5) chain B residue 217 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1260 source : AC2 6) chain B residue 8 type sequence K description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 7) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 8) chain B residue 11 type sequence G description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 9) chain B residue 43 type sequence G description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 10) chain B residue 44 type sequence G description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 11) chain B residue 45 type sequence G description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 12) chain B residue 65 type sequence L description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 13) chain B residue 66 type sequence R description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 14) chain B residue 158 type sequence N description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 15) chain B residue 161 type sequence A description BINDING SITE FOR RESIDUE X2W B 1259 source : AC4 16) chain B residue 8 type catalytic sequence K description 870 source MCSA : MCSA2 17) chain B residue 11 type catalytic sequence G description 870 source MCSA : MCSA2 18) chain B residue 45 type catalytic sequence G description 870 source MCSA : MCSA2 19) chain B residue 162 type catalytic sequence D description 870 source MCSA : MCSA2 20) chain B residue 217 type catalytic sequence K description 870 source MCSA : MCSA2 21) 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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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