eF-site ID 5vsl-A PDB Code 5vsl Chain A click to enlarge Title Crystal structure of viperin with bound [4Fe-4S] cluster and S-adenosylhomocysteine (SAH) Classification ANTIVIRAL PROTEIN Compound Radical S-adenosyl methionine domain-containing protein 2 Source (RSAD2_MOUSE) Sequence A:  TPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLL LLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALP SVSIVSNGSLIRERWFKDYGEYLDILAISCDSFDEQVNAL IGRGQGKKNHVENLQKLRRWCRDYKVAFKINSVINRFNVD EDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFL ISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRF LNCTDPSKSILDVGVEEAIKFS Description Functional site 1) chain A residue 84 type sequence C description binding site for residue SF4 A 401 source : AC1 2) chain A residue 86 type sequence Y description binding site for residue SF4 A 401 source : AC1 3) chain A residue 88 type sequence C description binding site for residue SF4 A 401 source : AC1 4) chain A residue 91 type sequence C description binding site for residue SF4 A 401 source : AC1 5) chain A residue 126 type sequence G description binding site for residue SF4 A 401 source : AC1 6) chain A residue 158 type sequence N description binding site for residue SF4 A 401 source : AC1 7) chain A residue 194 type sequence R description binding site for residue SF4 A 401 source : AC1 8) chain A residue 265 type sequence R description binding site for residue SF4 A 401 source : AC1 9) chain A residue 90 type sequence F description binding site for residue SAH A 402 source : AC2 10) chain A residue 91 type sequence C description binding site for residue SAH A 402 source : AC2 11) chain A residue 92 type sequence F description binding site for residue SAH A 402 source : AC2 12) chain A residue 124 type sequence S description binding site for residue SAH A 402 source : AC2 13) chain A residue 125 type sequence G description binding site for residue SAH A 402 source : AC2 14) chain A residue 126 type sequence G description binding site for residue SAH A 402 source : AC2 15) chain A residue 127 type sequence E description binding site for residue SAH A 402 source : AC2 16) chain A residue 156 type sequence V description binding site for residue SAH A 402 source : AC2 17) chain A residue 157 type sequence S description binding site for residue SAH A 402 source : AC2 18) chain A residue 158 type sequence N description binding site for residue SAH A 402 source : AC2 19) chain A residue 180 type sequence S description binding site for residue SAH A 402 source : AC2 20) chain A residue 194 type sequence R description binding site for residue SAH A 402 source : AC2 21) chain A residue 222 type sequence N description binding site for residue SAH A 402 source : AC2 22) chain A residue 224 type sequence V description binding site for residue SAH A 402 source : AC2 23) chain A residue 251 type sequence C description binding site for residue SAH A 402 source : AC2 24) chain A residue 252 type sequence L description binding site for residue SAH A 402 source : AC2 25) chain A residue 258 type sequence N description binding site for residue SAH A 402 source : AC2 26) chain A residue 84 type catalytic sequence C description 965 source MCSA : MCSA1 27) chain A residue 88 type catalytic sequence C description 965 source MCSA : MCSA1 28) chain A residue 91 type catalytic sequence C description 965 source MCSA : MCSA1 29) chain A residue 84 type BINDING sequence C description BINDING => ECO:0000269|PubMed:28607080, ECO:0007744|PDB:5VSL, ECO:0007744|PDB:5VSM source Swiss-Prot : SWS_FT_FI1 30) chain A residue 88 type BINDING sequence C description BINDING => ECO:0000269|PubMed:28607080, ECO:0007744|PDB:5VSL, ECO:0007744|PDB:5VSM source Swiss-Prot : SWS_FT_FI1 31) chain A residue 91 type BINDING sequence C description BINDING => ECO:0000269|PubMed:28607080, ECO:0007744|PDB:5VSL, ECO:0007744|PDB:5VSM source Swiss-Prot : SWS_FT_FI1 32) chain A residue 198 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q8WXG1 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 207 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q8WXG1 source Swiss-Prot : SWS_FT_FI3

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