eF-site ID 2a7r-A PDB Code 2a7r Chain A click to enlarge Title Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2) Classification OXIDOREDUCTASE Compound GMP reductase 2 Source Homo sapiens (Human) (GMPR2_HUMAN) Sequence A:  MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRN SKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVV TGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAG GVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVG AAKLKELSRRTTFIRVTQ Description (1)  GMP reductase 2 (E.C.1.7.1.7) Functional site 1) chain A residue 33 type sequence T description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 2) chain A residue 34 type sequence R description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 3) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 4) chain A residue 325 type sequence K description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 5) chain A residue 149 type sequence F description BINDING SITE FOR RESIDUE SO4 A 401 source : AC2 6) chain A residue 150 type sequence P description BINDING SITE FOR RESIDUE SO4 A 401 source : AC2 7) chain A residue 151 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 401 source : AC2 8) chain A residue 152 type sequence H description BINDING SITE FOR RESIDUE SO4 A 401 source : AC2 9) chain A residue 55 type sequence M description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 10) chain A residue 183 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 11) chain A residue 184 type sequence S description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 12) chain A residue 186 type sequence C description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 13) chain A residue 188 type sequence T description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 14) chain A residue 219 type sequence D description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 15) chain A residue 220 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 16) chain A residue 221 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 17) chain A residue 242 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 18) chain A residue 243 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 19) chain A residue 268 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 20) chain A residue 269 type sequence M description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 21) chain A residue 270 type sequence S description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 22) chain A residue 286 type sequence R description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 23) chain A residue 287 type sequence A description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 24) chain A residue 288 type sequence S description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 25) chain A residue 290 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 26) chain A residue 176-188 type prosite sequence IKVGIGPGSVCTT description IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGIGpGSVCtT source prosite : PS00487 27) chain A residue 186 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 188 type ACT_SITE sequence T description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 26 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 314 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 78 type BINDING sequence K description in other chain => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 129 type BINDING sequence D description in other chain => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 180 type BINDING sequence I description in other chain => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 269 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 285 type BINDING sequence Y description in other chain => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 181 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 183 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 186 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 189 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 40) chain A residue 219 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 41) chain A residue 242 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 42) chain A residue 268 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 286 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 291 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6

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