eF-site ID 2a7r-D PDB Code 2a7r Chain D 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 D:  MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRN SKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVV TGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM LGGMLAGHSESGGELIERDGKKYKLFYGKTVEVPFKGDVE HTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQ Description (1)  GMP reductase 2 (E.C.1.7.1.7) Functional site 1) chain D residue 33 type sequence T description BINDING SITE FOR RESIDUE SO4 D 3400 source : AC7 2) chain D residue 34 type sequence R description BINDING SITE FOR RESIDUE SO4 D 3400 source : AC7 3) chain D residue 35 type sequence S description BINDING SITE FOR RESIDUE SO4 D 3400 source : AC7 4) chain D residue 325 type sequence K description BINDING SITE FOR RESIDUE SO4 D 3400 source : AC7 5) chain D residue 183 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 6) chain D residue 184 type sequence S description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 7) chain D residue 220 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 8) chain D residue 221 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 9) chain D residue 222 type sequence C description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 10) chain D residue 242 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 11) chain D residue 243 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 12) chain D residue 186 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI1 13) chain D residue 188 type ACT_SITE sequence T description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI2 14) chain D residue 26 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI3 15) chain D residue 314 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI3 16) chain D 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 17) chain D 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 18) chain D 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 19) chain D residue 181 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 20) chain D residue 183 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 21) chain D residue 186 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 22) chain D residue 189 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 23) chain D residue 219 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 24) chain D residue 242 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 25) chain D residue 291 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6

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