eF-site ID 5e2d-A PDB Code 5e2d Chain A click to enlarge Title Crystal structure of IrCp*/Pd(allyl)-apo-Fr Classification METAL BINDING PROTEIN Compound Ferritin light chain Source (FRIL_HORSE) Sequence A:  SSQIRQNYSTEVEAAVNRLVNLYLRASYTYLSLGFYFDRD DVALEGVCHFFRELAEEKREGAERLLKMQNQRGGRALFQD LQKPSQDEWGTTLDAMKAAIVLEKSLNQALLDLHALGSAQ ADPHLCDFLESHFLDEEVKLIKKMGDHLTNIQRLVGSQAG LGEYLFERLTLK Description Functional site 1) chain A residue 49 type sequence H description binding site for residue IR3 A 201 source : AC1 2) chain A residue 49 type sequence H description binding site for residue IR3 A 202 source : AC2 3) chain A residue 128 type sequence F description binding site for residue IR3 A 203 source : AC3 4) chain A residue 114 type sequence H description binding site for residue IR3 A 204 source : AC4 5) chain A residue 118 type sequence S description binding site for residue IR3 A 204 source : AC4 6) chain A residue 126 type sequence C description binding site for residue IR3 A 204 source : AC4 7) chain A residue 49 type sequence H description binding site for residue IR3 A 205 source : AC5 8) chain A residue 45 type sequence E description binding site for residue SO4 A 207 source : AC7 9) chain A residue 143 type sequence K description binding site for residue SO4 A 207 source : AC7 10) chain A residue 146 type sequence D description binding site for residue SO4 A 207 source : AC7 11) chain A residue 147 type sequence H description binding site for residue SO4 A 207 source : AC7 12) chain A residue 6 type sequence Q description binding site for residue SO4 A 208 source : AC8 13) chain A residue 7 type sequence N description binding site for residue SO4 A 208 source : AC8 14) chain A residue 45 type sequence E description binding site for residue PLL A 209 source : AC9 15) chain A residue 48 type sequence C description binding site for residue PLL A 209 source : AC9 16) chain A residue 49 type sequence H description binding site for residue PLL A 209 source : AC9 17) chain A residue 52 type sequence R description binding site for residue PLL A 209 source : AC9 18) chain A residue 38 type sequence D description binding site for residue PLL A 210 source : AD1 19) chain A residue 45 type sequence E description binding site for residue PLL A 210 source : AD1 20) chain A residue 48 type sequence C description binding site for residue PLL A 210 source : AD1 21) chain A residue 114 type sequence H description binding site for residue PD A 211 source : AD2 22) chain A residue 126 type sequence C description binding site for residue PD A 211 source : AD2 23) chain A residue 80 type sequence D description binding site for residue CD A 212 source : AD3 24) chain A residue 80 type sequence D description binding site for residue CD A 212 source : AD3 25) chain A residue 82 type sequence Q description binding site for residue CD A 212 source : AD3 26) chain A residue 82 type sequence Q description binding site for residue CD A 212 source : AD3 27) chain A residue 122-142 type prosite sequence DPHLCDFLESHFLDEEVKLIK description FERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEshFLdeevklIK source prosite : PS00204 28) chain A residue 57-75 type prosite sequence EKREGAERLLKMQNQRGGR description FERRITIN_1 Ferritin iron-binding regions signature 1. EkREgaERLLkmQNqRgGR source prosite : PS00540 29) chain A residue 53 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 56 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 57 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 60 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 63 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000269|PubMed:7026284 source Swiss-Prot : SWS_FT_FI2

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