eF-site ID 2a7r-C PDB Code 2a7r Chain C 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 C:  MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRN SKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVV TGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYGK TVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRT TFIRVTQ Description (1)  GMP reductase 2 (E.C.1.7.1.7) Functional site 1) chain C residue 33 type sequence T description BINDING SITE FOR RESIDUE SO4 C 2400 source : AC5 2) chain C residue 34 type sequence R description BINDING SITE FOR RESIDUE SO4 C 2400 source : AC5 3) chain C residue 35 type sequence S description BINDING SITE FOR RESIDUE SO4 C 2400 source : AC5 4) chain C residue 149 type sequence F description BINDING SITE FOR RESIDUE SO4 C 2401 source : AC6 5) chain C residue 150 type sequence P description BINDING SITE FOR RESIDUE SO4 C 2401 source : AC6 6) chain C residue 151 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 2401 source : AC6 7) chain C residue 152 type sequence H description BINDING SITE FOR RESIDUE SO4 C 2401 source : AC6 8) chain C residue 53 type sequence A description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 9) chain C residue 55 type sequence M description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 10) chain C residue 184 type sequence S description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 11) chain C residue 186 type sequence C description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 12) chain C residue 188 type sequence T description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 13) chain C residue 219 type sequence D description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 14) chain C residue 220 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 15) chain C residue 221 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 16) chain C residue 242 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 17) chain C residue 243 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 18) chain C residue 268 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 19) chain C residue 269 type sequence M description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 20) chain C residue 270 type sequence S description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 21) chain C residue 290 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 22) chain C residue 186 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI1 23) chain C residue 188 type ACT_SITE sequence T description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 26 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI3 25) chain C residue 314 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469 source Swiss-Prot : SWS_FT_FI3 26) chain C 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 27) chain C 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 28) chain C 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 29) chain C 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 30) chain C residue 181 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 31) chain C residue 183 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 32) chain C residue 186 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 33) chain C residue 189 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 34) chain C residue 219 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 35) chain C residue 242 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 36) chain C residue 268 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 37) chain C residue 291 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6

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