eF-site ID 3pvn-ABCDEPQRST PDB Code 3pvn Chain A, B, C, D, E, P, Q, R, S, T click to enlarge Title Triclinic form of Human C-Reactive Protein in complex with Zinc Classification IMMUNE SYSTEM Compound C-reactive protein Source Homo sapiens (Human) (CRP_HUMAN) Sequence A:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP B:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP C:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP D:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP E:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP P:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP Q:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP R:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP S:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP T:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP Description Functional site 1) chain A residue 60 type sequence D description BINDING SITE FOR RESIDUE CA A 5001 source : AC1 2) chain A residue 61 type sequence N description BINDING SITE FOR RESIDUE CA A 5001 source : AC1 3) chain A residue 138 type sequence E description BINDING SITE FOR RESIDUE CA A 5001 source : AC1 4) chain A residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA A 5001 source : AC1 5) chain A residue 140 type sequence D description BINDING SITE FOR RESIDUE CA A 5001 source : AC1 6) chain A residue 138 type sequence E description BINDING SITE FOR RESIDUE CA A 5002 source : AC2 7) chain A residue 140 type sequence D description BINDING SITE FOR RESIDUE CA A 5002 source : AC2 8) chain A residue 147 type sequence E description BINDING SITE FOR RESIDUE CA A 5002 source : AC2 9) chain A residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA A 5002 source : AC2 10) chain A residue 38 type sequence H description BINDING SITE FOR RESIDUE ZN A 6001 source : AC3 11) chain B residue 138 type sequence E description BINDING SITE FOR RESIDUE CA B 5003 source : AC4 12) chain B residue 140 type sequence D description BINDING SITE FOR RESIDUE CA B 5003 source : AC4 13) chain B residue 147 type sequence E description BINDING SITE FOR RESIDUE CA B 5003 source : AC4 14) chain B residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA B 5003 source : AC4 15) chain B residue 60 type sequence D description BINDING SITE FOR RESIDUE CA B 5004 source : AC5 16) chain B residue 61 type sequence N description BINDING SITE FOR RESIDUE CA B 5004 source : AC5 17) chain B residue 138 type sequence E description BINDING SITE FOR RESIDUE CA B 5004 source : AC5 18) chain B residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA B 5004 source : AC5 19) chain B residue 140 type sequence D description BINDING SITE FOR RESIDUE CA B 5004 source : AC5 20) chain C residue 138 type sequence E description BINDING SITE FOR RESIDUE CA C 5005 source : AC6 21) chain C residue 140 type sequence D description BINDING SITE FOR RESIDUE CA C 5005 source : AC6 22) chain C residue 147 type sequence E description BINDING SITE FOR RESIDUE CA C 5005 source : AC6 23) chain C residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA C 5005 source : AC6 24) chain S residue 70 type sequence D description BINDING SITE FOR RESIDUE CA C 5005 source : AC6 25) chain C residue 60 type sequence D description BINDING SITE FOR RESIDUE CA C 5006 source : AC7 26) chain C residue 61 type sequence N description BINDING SITE FOR RESIDUE CA C 5006 source : AC7 27) chain C residue 138 type sequence E description BINDING SITE FOR RESIDUE CA C 5006 source : AC7 28) chain C residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA C 5006 source : AC7 29) chain C residue 140 type sequence D description BINDING SITE FOR RESIDUE CA C 5006 source : AC7 30) chain D residue 60 type sequence D description BINDING SITE FOR RESIDUE CA D 5007 source : AC8 31) chain D residue 61 type sequence N description BINDING SITE FOR RESIDUE CA D 5007 source : AC8 32) chain D residue 138 type sequence E description BINDING SITE FOR RESIDUE CA D 5007 source : AC8 33) chain D residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA D 5007 source : AC8 34) chain D residue 140 type sequence D description BINDING SITE FOR RESIDUE CA D 5007 source : AC8 35) chain D residue 138 type sequence E description BINDING SITE FOR RESIDUE CA D 5008 source : AC9 36) chain D residue 140 type sequence D description BINDING SITE FOR RESIDUE CA D 5008 source : AC9 37) chain D residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA D 5008 source : AC9 38) chain E residue 60 type sequence D description BINDING SITE FOR RESIDUE CA E 5009 source : BC1 39) chain E residue 61 type sequence N description BINDING SITE FOR RESIDUE CA E 5009 source : BC1 40) chain E residue 138 type sequence E description BINDING SITE FOR RESIDUE CA E 5009 source : BC1 41) chain E residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA E 5009 source : BC1 42) chain E residue 140 type sequence D description BINDING SITE FOR RESIDUE CA E 5009 source : BC1 43) chain E residue 138 type sequence E description BINDING SITE FOR RESIDUE CA E 5010 source : BC2 44) chain E residue 140 type sequence D description BINDING SITE FOR RESIDUE CA E 5010 source : BC2 45) chain E residue 147 type sequence E description BINDING SITE FOR RESIDUE CA E 5010 source : BC2 46) chain E residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA E 5010 source : BC2 47) chain P residue 60 type sequence D description BINDING SITE FOR RESIDUE CA F 5011 source : BC3 48) chain P residue 140 type sequence D description BINDING SITE FOR RESIDUE CA F 5012 source : BC4 49) chain P residue 60 type sequence D description BINDING SITE FOR RESIDUE CA P 5031 source : DC7 50) chain P residue 61 type sequence N description BINDING SITE FOR RESIDUE CA P 5031 source : DC7 51) chain P residue 138 type sequence E description BINDING SITE FOR RESIDUE CA P 5031 source : DC7 52) chain P residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA P 5031 source : DC7 53) chain P residue 140 type sequence D description BINDING SITE FOR RESIDUE CA P 5031 source : DC7 54) chain P residue 138 type sequence E description BINDING SITE FOR RESIDUE CA P 5032 source : DC8 55) chain P residue 140 type sequence D description BINDING SITE FOR RESIDUE CA P 5032 source : DC8 56) chain P residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA P 5032 source : DC8 57) chain Q residue 138 type sequence E description BINDING SITE FOR RESIDUE CA Q 5033 source : DC9 58) chain Q residue 140 type sequence D description BINDING SITE FOR RESIDUE CA Q 5033 source : DC9 59) chain Q residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA Q 5033 source : DC9 60) chain Q residue 60 type sequence D description BINDING SITE FOR RESIDUE CA Q 5034 source : EC1 61) chain Q residue 61 type sequence N description BINDING SITE FOR RESIDUE CA Q 5034 source : EC1 62) chain Q residue 138 type sequence E description BINDING SITE FOR RESIDUE CA Q 5034 source : EC1 63) chain Q residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA Q 5034 source : EC1 64) chain Q residue 140 type sequence D description BINDING SITE FOR RESIDUE CA Q 5034 source : EC1 65) chain R residue 60 type sequence D description BINDING SITE FOR RESIDUE CA R 5035 source : EC2 66) chain R residue 61 type sequence N description BINDING SITE FOR RESIDUE CA R 5035 source : EC2 67) chain R residue 138 type sequence E description BINDING SITE FOR RESIDUE CA R 5035 source : EC2 68) chain R residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA R 5035 source : EC2 69) chain R residue 140 type sequence D description BINDING SITE FOR RESIDUE CA R 5035 source : EC2 70) chain R residue 138 type sequence E description BINDING SITE FOR RESIDUE CA R 5036 source : EC3 71) chain R residue 140 type sequence D description BINDING SITE FOR RESIDUE CA R 5036 source : EC3 72) chain R residue 147 type sequence E description BINDING SITE FOR RESIDUE CA R 5036 source : EC3 73) chain R residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA R 5036 source : EC3 74) chain S residue 60 type sequence D description BINDING SITE FOR RESIDUE CA S 5037 source : EC4 75) chain S residue 61 type sequence N description BINDING SITE FOR RESIDUE CA S 5037 source : EC4 76) chain S residue 138 type sequence E description BINDING SITE FOR RESIDUE CA S 5037 source : EC4 77) chain S residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA S 5037 source : EC4 78) chain S residue 140 type sequence D description BINDING SITE FOR RESIDUE CA S 5037 source : EC4 79) chain S residue 138 type sequence E description BINDING SITE FOR RESIDUE CA S 5038 source : EC5 80) chain S residue 140 type sequence D description BINDING SITE FOR RESIDUE CA S 5038 source : EC5 81) chain S residue 147 type sequence E description BINDING SITE FOR RESIDUE CA S 5038 source : EC5 82) chain S residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA S 5038 source : EC5 83) chain S residue 38 type sequence H description BINDING SITE FOR RESIDUE ZN S 6004 source : EC6 84) chain T residue 138 type sequence E description BINDING SITE FOR RESIDUE CA T 5039 source : EC7 85) chain T residue 140 type sequence D description BINDING SITE FOR RESIDUE CA T 5039 source : EC7 86) chain T residue 147 type sequence E description BINDING SITE FOR RESIDUE CA T 5039 source : EC7 87) chain T residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA T 5039 source : EC7 88) chain T residue 60 type sequence D description BINDING SITE FOR RESIDUE CA T 5040 source : EC8 89) chain T residue 61 type sequence N description BINDING SITE FOR RESIDUE CA T 5040 source : EC8 90) chain T residue 138 type sequence E description BINDING SITE FOR RESIDUE CA T 5040 source : EC8 91) chain T residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA T 5040 source : EC8 92) chain T residue 140 type sequence D description BINDING SITE FOR RESIDUE CA T 5040 source : EC8 93) chain D residue 69 type sequence K description BINDING SITE FOR RESIDUE ZN T 6005 source : EC9 94) chain D residue 70 type sequence D description BINDING SITE FOR RESIDUE ZN T 6005 source : EC9 95) chain T residue 60 type sequence D description BINDING SITE FOR RESIDUE ZN T 6005 source : EC9 96) chain A residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 97) chain B residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 98) chain Q residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 99) chain Q residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 100) chain Q residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 101) chain R residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 102) chain R residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 103) chain R residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 104) chain R residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 105) chain R residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 106) chain R residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 107) chain S residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 108) chain B residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 109) chain S residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 110) chain S residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 111) chain S residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 112) chain S residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 113) chain S residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 114) chain T residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 115) chain T residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 116) chain T residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 117) chain T residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 118) chain T residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 119) chain B residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 120) chain T residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 121) chain C residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 122) chain C residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 123) chain C residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 124) chain C residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 125) chain C residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 126) chain C residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 127) chain D residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 128) chain A residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 129) chain D residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 130) chain D residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 131) chain D residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 132) chain D residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 133) chain D residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 134) chain E residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 135) chain E residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 136) chain E residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 137) chain E residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 138) chain E residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 139) chain A residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 140) chain E residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 141) chain A residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 142) chain A residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 143) chain A residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 144) chain B residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 145) chain B residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 146) chain B residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 147) chain P residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 148) chain P residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 149) chain P residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 150) chain P residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 151) chain P residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 152) chain P residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 153) chain Q residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 154) chain Q residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 155) chain Q residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 156) chain A residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 157) chain P residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 158) chain Q residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 159) chain R residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 160) chain S residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 161) chain B residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 162) chain T residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 163) chain C residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 164) chain D residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 165) chain E residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 166) chain A residue 95-102 type prosite sequence HICTSWES description PTX_1 Pentraxin domain signature. HiCtSWeS source prosite : PS00289

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