eF-site ID 6mv9-AB PDB Code 6mv9 Chain A, B click to enlarge Title X-ray crystal structure of Bacillus subtilis ribonucleotide reductase NrdE alpha subunit with TTP and ADP Classification OXIDOREDUCTASE Compound Ribonucleoside-diphosphate reductase Source (A0A162Q3J9_BACIU) Sequence A:  KWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVF FHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEVFKTAYAK KFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVAL FFANGDTEKAKEYVNLMINQEYQPSTPTFLNAGRKRRGEL VSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLR AKGEAIKDVENATKGVVGVMKLLDNAFRYADQMGQRQGSG AAYLNIFHRDINDFLDTKKISAVKTLSIGVVIPDKFVELA REDKAAYVFYPHTIYKEYGQHMDEMDMNEMYDKFVDNPRV KKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNH ISKVKFSNLCSEVLQASQVSSYTDYDEEDEIGLDISCNLG SLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVR RANKAMKSIGLGAMNLHGYLAQNGIAYESPEARDFANTFF MMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYV STDFSPKYEKIANLFEGMHIPTTEDWKKLKAFVAEHGMYH SYRLCIAPTGSISYVQSSTASVMPIMERIEEKTYYPMPGL ASNNWFFYKEAYDMDMFKVVDMIATIQQHIDQGISFTLFL KDTMTTRDLNRIDLYAHHRGIKTIYYASCLSCVV B:  PKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTV FFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEVFKTAYA KKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVA LFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAGRKRRGE LVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKL RAKGEAIKDVENATKGVVGVMKLLDNAFRYASGAAYLNIF HRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELARE DKAAYVFYPHTIYKEYGQHMDEMDMNEMYDKFVDNPRVKK EKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHIS KVKFSNLCSEVLQASQVSSYTDYDEEDEIGLDISCNLGSL NILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRA NKAMKSIGLGAMNLHGYLAQNGIAYESPEARDFANTFFMM VNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVST DFSPKYEKIANLFEGMHIPTTEDWKKLKAFVAEHGMYHSY RLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYP MPGLASNNWFFYKEAYDMDMFKVVDMIATIQQHIDQGISF TLFLKDTMTTRDLNRIDLYAHHRGIKTIYYASCLSCVV Description Functional site 1) chain A residue 177 type sequence D description binding site for residue TTP A 801 source : AC1 2) chain A residue 178 type sequence S description binding site for residue TTP A 801 source : AC1 3) chain A residue 179 type sequence L description binding site for residue TTP A 801 source : AC1 4) chain A residue 182 type sequence I description binding site for residue TTP A 801 source : AC1 5) chain A residue 207 type sequence R description binding site for residue TTP A 801 source : AC1 6) chain A residue 213 type sequence I description binding site for residue TTP A 801 source : AC1 7) chain A residue 214 type sequence K description binding site for residue TTP A 801 source : AC1 8) chain A residue 220 type sequence T description binding site for residue TTP A 801 source : AC1 9) chain A residue 221 type sequence K description binding site for residue TTP A 801 source : AC1 10) chain B residue 194 type sequence K description binding site for residue TTP A 801 source : AC1 11) chain B residue 236 type sequence Y description binding site for residue TTP A 801 source : AC1 12) chain B residue 237 type sequence A description binding site for residue TTP A 801 source : AC1 13) chain A residue 33 type sequence V description binding site for residue ADP A 802 source : AC2 14) chain A residue 34 type sequence H description binding site for residue ADP A 802 source : AC2 15) chain A residue 37 type sequence F description binding site for residue ADP A 802 source : AC2 16) chain A residue 42 type sequence N description binding site for residue ADP A 802 source : AC2 17) chain A residue 89 type sequence F description binding site for residue ADP A 802 source : AC2 18) chain A residue 90 type sequence R description binding site for residue ADP A 802 source : AC2 19) chain A residue 91 type sequence F description binding site for residue ADP A 802 source : AC2 20) chain A residue 194 type sequence K description binding site for residue TTP B 801 source : AC4 21) chain A residue 236 type sequence Y description binding site for residue TTP B 801 source : AC4 22) chain A residue 237 type sequence A description binding site for residue TTP B 801 source : AC4 23) chain B residue 177 type sequence D description binding site for residue TTP B 801 source : AC4 24) chain B residue 178 type sequence S description binding site for residue TTP B 801 source : AC4 25) chain B residue 179 type sequence L description binding site for residue TTP B 801 source : AC4 26) chain B residue 182 type sequence I description binding site for residue TTP B 801 source : AC4 27) chain B residue 207 type sequence R description binding site for residue TTP B 801 source : AC4 28) chain B residue 213 type sequence I description binding site for residue TTP B 801 source : AC4 29) chain B residue 214 type sequence K description binding site for residue TTP B 801 source : AC4 30) chain B residue 220 type sequence T description binding site for residue TTP B 801 source : AC4 31) chain B residue 221 type sequence K description binding site for residue TTP B 801 source : AC4 32) chain B residue 34 type sequence H description binding site for residue ADP B 802 source : AC5 33) chain B residue 37 type sequence F description binding site for residue ADP B 802 source : AC5 34) chain B residue 42 type sequence N description binding site for residue ADP B 802 source : AC5 35) chain B residue 90 type sequence R description binding site for residue ADP B 802 source : AC5 36) chain B residue 91 type sequence F description binding site for residue ADP B 802 source : AC5 37) chain A residue 558-580 type prosite sequence WKKLKAFVAEHGMYHSYRLCIAP description RIBORED_LARGE Ribonucleotide reductase large subunit signature. WkkLkafvaehGMYHsyrLCiaP source prosite : PS00089 38) chain A residue 380 type ACT_SITE sequence N description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 384 type ACT_SITE sequence E description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 380 type ACT_SITE sequence N description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 384 type ACT_SITE sequence E description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 382 type ACT_SITE sequence C description Cysteine radical intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 382 type ACT_SITE sequence C description Cysteine radical intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 153 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 580 type BINDING sequence P description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 46) chain A residue 169 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 198 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 380 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 580 type BINDING sequence P description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 153 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 169 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 52) chain B residue 198 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 53) chain B residue 380 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 54) chain A residue 170 type SITE sequence C description Important for hydrogen atom transfer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 409 type SITE sequence C description Important for hydrogen atom transfer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 56) chain B residue 170 type SITE sequence C description Important for hydrogen atom transfer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 57) chain B residue 409 type SITE sequence C description Important for hydrogen atom transfer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 58) chain A residue 177 type SITE sequence D description Allosteric effector binding => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 207 type SITE sequence R description Allosteric effector binding => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 60) chain B residue 177 type SITE sequence D description Allosteric effector binding => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 207 type SITE sequence R description Allosteric effector binding => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 62) chain A residue 683 type SITE sequence Y description Important for electron transfer => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 63) chain A residue 684 type SITE sequence Y description Important for electron transfer => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 64) chain B residue 683 type SITE sequence Y description Important for electron transfer => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 65) chain B residue 684 type SITE sequence Y description Important for electron transfer => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 66) chain A residue 695 type SITE sequence C description Interacts with thioredoxin/glutaredoxin => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 67) chain A residue 698 type SITE sequence C description Interacts with thioredoxin/glutaredoxin => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 68) chain B residue 695 type SITE sequence C description Interacts with thioredoxin/glutaredoxin => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 69) chain B residue 698 type SITE sequence C description Interacts with thioredoxin/glutaredoxin => ECO:0000250 source Swiss-Prot : SWS_FT_FI7

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