eF-site ID 5ax8-A PDB Code 5ax8 Chain A click to enlarge Title Recombinant expression, purification and preliminary crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase Classification TRANSFERASE Compound Aspartate aminotransferase, mitochondrial Source Homo sapiens (Human) (AATM_HUMAN) Sequence A:  SSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRD DNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKAS AELALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFF KFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGF DFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEI ATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGI NVCLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLK ILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKGMAD RIIGMRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPE QVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVT K Description Functional site 1) chain A residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI2 2) chain A residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI3 3) chain A residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI3 4) chain A residue 302 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 345 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI3 6) chain A residue 364 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI3 7) chain A residue 387 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI3 8) chain A residue 65 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 9) chain A residue 162 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 215 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 407 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 73 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 396 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 404 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 15) chain A residue 90 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 159 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 185 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 20) chain A residue 296 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 338 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 363 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 276-289 type prosite sequence SYAKNMGLYGERVG description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYAKnmGLyGERVG source prosite : PS00105 24) chain A residue 309 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P12344 source Swiss-Prot : SWS_FT_FI10 25) chain A residue 313 type MOD_RES sequence R description Asymmetric dimethylarginine => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI11 26) chain A residue 333 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI12 27) chain A residue 96 type MOD_RES sequence Y description Phosphotyrosine; alternate => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 143 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 29) chain A residue 227 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI7 30) chain A residue 234 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 31) chain A residue 279 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P05202 source Swiss-Prot : SWS_FT_FI9

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