eF-site ID 6h2v-C PDB Code 6h2v Chain C click to enlarge Title Crystal structure of human METTL5-TRMT112 complex, the 18S rRNA m6A1832 methyltransferase at 2.5A resolution Classification TRANSFERASE Compound Methyltransferase-like protein 5 Source (TR112_HUMAN) Sequence C:  KVRLKELESRLQQVDGFEKPKLLLEQYPTRPHIAACMLYT IHNTYDDIENKVVADLGCGCGVLSIGTAMLGAGLCVGFDI DEDALEIFNRNAEEFELTNIDMVQCDVCLLSNRMSKSFDT VIMNPPFGTDMAFLKTALEMARTAVYSLHKSSTREHVQKK AAEWKIKIDIIAELRYDLPAVDIEVDLIRFSFHH Description Functional site 1) chain C residue 19 type sequence F description binding site for residue SAM C 301 source : AC8 2) chain C residue 26 type sequence L description binding site for residue SAM C 301 source : AC8 3) chain C residue 27 type sequence E description binding site for residue SAM C 301 source : AC8 4) chain C residue 28 type sequence Q description binding site for residue SAM C 301 source : AC8 5) chain C residue 29 type sequence Y description binding site for residue SAM C 301 source : AC8 6) chain C residue 30 type sequence P description binding site for residue SAM C 301 source : AC8 7) chain C residue 31 type sequence T description binding site for residue SAM C 301 source : AC8 8) chain C residue 59 type sequence G description binding site for residue SAM C 301 source : AC8 9) chain C residue 60 type sequence C description binding site for residue SAM C 301 source : AC8 10) chain C residue 61 type sequence G description binding site for residue SAM C 301 source : AC8 11) chain C residue 62 type sequence C description binding site for residue SAM C 301 source : AC8 12) chain C residue 64 type sequence V description binding site for residue SAM C 301 source : AC8 13) chain C residue 81 type sequence D description binding site for residue SAM C 301 source : AC8 14) chain C residue 82 type sequence I description binding site for residue SAM C 301 source : AC8 15) chain C residue 107 type sequence C description binding site for residue SAM C 301 source : AC8 16) chain C residue 108 type sequence D description binding site for residue SAM C 301 source : AC8 17) chain C residue 109 type sequence V description binding site for residue SAM C 301 source : AC8 18) chain C residue 126 type sequence N description binding site for residue SAM C 301 source : AC8 19) chain C residue 128 type sequence P description binding site for residue SAM C 301 source : AC8 20) chain C residue 32 type sequence R description binding site for residue PG0 C 302 source : AC9 21) chain C residue 33 type sequence P description binding site for residue PG0 C 302 source : AC9 22) chain C residue 34 type sequence H description binding site for residue PG0 C 302 source : AC9 23) chain C residue 151 type sequence T description binding site for residue SO4 C 303 source : AD1 24) chain C residue 206 type sequence R description binding site for residue SO4 C 303 source : AD1 25) chain C residue 208 type sequence S description binding site for residue SO4 C 303 source : AD1 26) chain C residue 211 type sequence H description binding site for residue SO4 C 303 source : AD1 27) chain C residue 175 type sequence K description binding site for residue SO4 C 304 source : AD2 28) chain C residue 210 type sequence H description binding site for residue SO4 C 304 source : AD2 29) chain C residue 211 type sequence H description binding site for residue SO4 C 304 source : AD2 30) chain C residue 91 type sequence N description binding site for residue EDO D 201 source : AD3 31) chain C residue 103 type sequence D description binding site for residue EDO D 201 source : AD3 32) chain C residue 104 type sequence M description binding site for residue EDO D 201 source : AD3 33) chain C residue 95 type sequence E description binding site for residue PG0 D 202 source : AD4 34) chain C residue 108 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI1 35) chain C residue 31 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI1 36) chain C residue 59 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI1 37) chain C residue 81 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 28 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 64 type BINDING sequence V description BINDING => ECO:0000269|PubMed:31328227, ECO:0007744|PDB:6H2V source Swiss-Prot : SWS_FT_FI3

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