eF-site ID 2a7r-ABCD PDB Code 2a7r Chain A, B, C, 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 A:  MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRN SKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVV TGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAG GVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVG AAKLKELSRRTTFIRVTQ B:  MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRN SKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVV TGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAG GVAEYRSEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGA AKLKELSRRTTFIRVTQ C:  MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRN SKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVV TGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYGK TVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRT TFIRVTQ D:  MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRN SKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVV TGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM LGGMLAGHSESGGELIERDGKKYKLFYGKTVEVPFKGDVE HTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQ 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 B residue 33 type sequence T description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 10) chain B residue 34 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 11) chain B residue 35 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 12) chain B residue 323 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 13) chain B residue 325 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1400 source : AC3 14) chain B residue 149 type sequence F description BINDING SITE FOR RESIDUE SO4 B 1401 source : AC4 15) chain B residue 150 type sequence P description BINDING SITE FOR RESIDUE SO4 B 1401 source : AC4 16) chain B residue 151 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 1401 source : AC4 17) chain B residue 152 type sequence H description BINDING SITE FOR RESIDUE SO4 B 1401 source : AC4 18) chain C residue 33 type sequence T description BINDING SITE FOR RESIDUE SO4 C 2400 source : AC5 19) chain C residue 34 type sequence R description BINDING SITE FOR RESIDUE SO4 C 2400 source : AC5 20) chain C residue 35 type sequence S description BINDING SITE FOR RESIDUE SO4 C 2400 source : AC5 21) chain C residue 149 type sequence F description BINDING SITE FOR RESIDUE SO4 C 2401 source : AC6 22) chain C residue 150 type sequence P description BINDING SITE FOR RESIDUE SO4 C 2401 source : AC6 23) chain C residue 151 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 2401 source : AC6 24) chain C residue 152 type sequence H description BINDING SITE FOR RESIDUE SO4 C 2401 source : AC6 25) chain D residue 33 type sequence T description BINDING SITE FOR RESIDUE SO4 D 3400 source : AC7 26) chain D residue 34 type sequence R description BINDING SITE FOR RESIDUE SO4 D 3400 source : AC7 27) chain D residue 35 type sequence S description BINDING SITE FOR RESIDUE SO4 D 3400 source : AC7 28) chain D residue 325 type sequence K description BINDING SITE FOR RESIDUE SO4 D 3400 source : AC7 29) chain D residue 183 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 30) chain D residue 184 type sequence S description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 31) chain D residue 220 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 32) chain D residue 221 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 33) chain D residue 222 type sequence C description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 34) chain D residue 242 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 35) chain D residue 243 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3500 source : AC8 36) chain A residue 55 type sequence M description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 37) chain A residue 183 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 38) chain A residue 184 type sequence S description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 39) chain A residue 186 type sequence C description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 40) chain A residue 188 type sequence T description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 41) chain A residue 219 type sequence D description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 42) chain A residue 220 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 43) chain A residue 221 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 44) chain A residue 242 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 45) chain A residue 243 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 46) chain A residue 268 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 47) chain A residue 269 type sequence M description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 48) chain A residue 270 type sequence S description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 49) chain A residue 286 type sequence R description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 50) chain A residue 287 type sequence A description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 51) chain A residue 288 type sequence S description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 52) chain A residue 290 type sequence G description BINDING SITE FOR RESIDUE 5GP A 500 source : AC9 53) chain B residue 53 type sequence A description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 54) chain B residue 55 type sequence M description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 55) chain B residue 183 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 56) chain B residue 184 type sequence S description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 57) chain B residue 186 type sequence C description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 58) chain B residue 188 type sequence T description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 59) chain B residue 219 type sequence D description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 60) chain B residue 220 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 61) chain B residue 221 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 62) chain B residue 242 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 63) chain B residue 243 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 64) chain B residue 268 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 65) chain B residue 270 type sequence S description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 66) chain B residue 286 type sequence R description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 67) chain B residue 288 type sequence S description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 68) chain B residue 290 type sequence G description BINDING SITE FOR RESIDUE 5GP B 500 source : BC1 69) chain C residue 53 type sequence A description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 70) chain C residue 55 type sequence M description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 71) chain C residue 184 type sequence S description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 72) chain C residue 186 type sequence C description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 73) chain C residue 188 type sequence T description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 74) chain C residue 219 type sequence D description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 75) chain C residue 220 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 76) chain C residue 221 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 77) chain C residue 242 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 78) chain C residue 243 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 79) chain C residue 268 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 80) chain C residue 269 type sequence M description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 81) chain C residue 270 type sequence S description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 82) chain C residue 290 type sequence G description BINDING SITE FOR RESIDUE 5GP C 500 source : BC2 83) chain A residue 176-188 type prosite sequence IKVGIGPGSVCTT description IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGIGpGSVCtT source prosite : PS00487 84) chain A residue 186 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI1 85) chain B residue 186 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI1 86) chain C residue 186 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI1 87) chain D residue 186 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI1 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) 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 95) 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 96) 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 97) 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 98) 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 99) 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 100) 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 101) 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 102) 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 103) 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 104) 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 105) 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 106) 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 107) 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 108) 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 109) 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 110) 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 111) 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 112) 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 113) 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 114) 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 115) 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 116) 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 117) chain A residue 181 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 118) chain B residue 183 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 119) chain B residue 186 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 120) chain B residue 189 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 121) chain B residue 219 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 122) chain B residue 242 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 123) chain B residue 268 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 124) chain B residue 286 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 125) chain C residue 181 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 126) chain C residue 183 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 127) chain C residue 186 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 128) chain A residue 183 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 129) chain C residue 189 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 130) chain C residue 219 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 131) chain C residue 242 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 132) chain C residue 268 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 133) chain D residue 181 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 134) chain D residue 183 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 135) chain D residue 186 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 136) chain D residue 189 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 137) chain D residue 219 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 138) chain A residue 186 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 139) chain D residue 242 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 140) chain A residue 189 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 141) chain A residue 219 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 142) chain A residue 242 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 143) chain A residue 268 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 144) chain A residue 286 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 145) chain B residue 181 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03195 source Swiss-Prot : SWS_FT_FI5 146) chain A residue 291 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 147) chain B residue 291 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 148) chain C residue 291 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 149) 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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