eF-site ID 6d5x-B PDB Code 6d5x Chain B click to enlarge Title Structure of Human ATP:Cobalamin Adenosyltransferase bound to ATP, Adenosylcobalamin, and Triphosphate Classification TRANSFERASE Compound Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial Source (MMAB_HUMAN) Sequence B:  KIYTKTGDKGFSSTFTGERRPKDDQVFEAVGTTDELSSAI GFALELVTEKGHTFAEELQKIQCTLQDVGSALATPCSSAR EAHLKYTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGG KISSALHFCRAVCRRAERRVVPLVQMGETDANVAKFLNRL SDYLFTLARYAAMKEGNQEKIYM Description Functional site 1) chain B residue 190 type sequence R description binding site for residue 5AD B 301 source : AC6 2) chain B residue 193 type sequence E description binding site for residue 5AD B 301 source : AC6 3) chain B residue 194 type sequence R description binding site for residue 5AD B 301 source : AC6 4) chain B residue 57 type sequence K description binding site for residue B12 B 302 source : AC7 5) chain B residue 167 type sequence L description binding site for residue B12 B 302 source : AC7 6) chain B residue 168 type sequence T description binding site for residue B12 B 302 source : AC7 7) chain B residue 170 type sequence F description binding site for residue B12 B 302 source : AC7 8) chain B residue 171 type sequence I description binding site for residue B12 B 302 source : AC7 9) chain B residue 186 type sequence R description binding site for residue B12 B 302 source : AC7 10) chain B residue 190 type sequence R description binding site for residue B12 B 302 source : AC7 11) chain B residue 217 type sequence S description binding site for residue B12 B 302 source : AC7 12) chain B residue 221 type sequence F description binding site for residue B12 B 302 source : AC7 13) chain B residue 108 type sequence H description binding site for residue SO4 B 303 source : AC8 14) chain B residue 109 type sequence T description binding site for residue SO4 B 303 source : AC8 15) chain B residue 110 type sequence F description binding site for residue SO4 B 303 source : AC8 16) chain B residue 226 type sequence Y description binding site for residue SO4 B 303 source : AC8 17) chain B residue 60 type sequence T description binding site for residue ATP C 301 source : AC9 18) chain B residue 61 type sequence K description binding site for residue ATP C 301 source : AC9 19) chain B residue 62 type sequence T description binding site for residue ATP C 301 source : AC9 20) chain B residue 63 type sequence G description binding site for residue ATP C 301 source : AC9 21) chain B residue 68 type sequence S description binding site for residue ATP C 301 source : AC9 22) chain B residue 69 type sequence S description binding site for residue ATP C 301 source : AC9 23) chain B residue 78 type sequence K description binding site for residue ATP C 301 source : AC9 24) chain B residue 83 type sequence F description binding site for residue ATP C 301 source : AC9 25) chain B residue 211 type sequence K description binding site for residue SO4 C 305 source : AD4 26) chain B residue 215 type sequence R description binding site for residue SO4 C 305 source : AD4 27) chain B residue 214 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17176040 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 60 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17176040 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 68 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17176040 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 78 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17176040 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 190 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17176040 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 134 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 211 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9D273 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 230 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9D273 source Swiss-Prot : SWS_FT_FI4

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