eF-site ID 2a7r-B PDB Code 2a7r Chain B 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 B:  MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRN SKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVV TGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAG GVAEYRSEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGA AKLKELSRRTTFIRVTQ Description (1)  GMP reductase 2 (E.C.1.7.1.7) Functional site 1) chain B residue 33 type sequence T description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 2) chain B residue 34 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 3) chain B residue 35 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 4) chain B residue 323 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 5) chain B residue 325 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 6) chain B residue 149 type sequence F description BINDING SITE FOR RESIDUE SO4 B 1401 source : AC4 7) chain B residue 150 type sequence P description BINDING SITE FOR RESIDUE SO4 B 1401 source : AC4 8) chain B residue 151 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 1401 source : AC4 9) chain B residue 152 type sequence H description BINDING SITE FOR RESIDUE SO4 B 1401 source : AC4 10) chain B residue 53 type sequence A description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 11) chain B residue 55 type sequence M description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 12) chain B residue 183 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 13) chain B residue 184 type sequence S description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 14) chain B residue 186 type sequence C description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 15) chain B residue 188 type sequence T description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 16) chain B residue 219 type sequence D description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 17) chain B residue 220 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 18) chain B residue 221 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 19) chain B residue 242 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 20) chain B residue 243 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 21) chain B residue 268 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 22) chain B residue 270 type sequence S description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 23) chain B residue 286 type sequence R description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 24) chain B residue 288 type sequence S description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 25) chain B residue 290 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 26) chain B residue 186 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 188 type ACT_SITE sequence T description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 26 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 314 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI3 30) chain B 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 31) chain B 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 B 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 B 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 B 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 B residue 183 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 36) chain B residue 186 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 37) chain B residue 189 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 219 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 39) chain B residue 242 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 40) chain B residue 268 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 41) chain B residue 286 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 42) chain B residue 181 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 43) chain B residue 291 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6

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