eF-site ID 2c8n-ABCDEF PDB Code 2c8n Chain A, B, C, D, E, F click to enlarge Title The Structure of a family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum in complex with 1,3-linked arabinoside of xylobiose. Classification HYDROLASE Compound ALPHA-L-ARABINOFURANOSIDASE Source (Q4CJG5_CLOTM) Sequence A:  KKARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPG NSKSDEDGFRKDVIELVKELNVPIIRYPGGNFVSNYFWED GVGPVEDRPRRLDLAWKSIEPNQVGINEFAKWCKKVNAEI MMAVNLGTRGISDACNLLEYCNHPGGSKYSDMRIKHGVKE PHNIKVWCLGNAMDGPWQVGHKTMDEYGRIAEETARAMKM IDPSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISL HQYYGNKENDTADFLAKSDDLDDFIRSVIATCDYIKAKKR SKKDIYLSFDEWNVWYHSNNEDANIMQNEPWRIAPPLLED IYTFEDALLVGLMLITLMKHADRIKIACLAQLINVIAPIV TERNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDT SKHEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSD VRGMKDYRLLEHIVLEHQDLKIRNSVNGEEVYPKNSDKSS FDDGILTSMLRRASWNVIRIG B:  KARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPGN SKSDEDGFRKDVIELVKELNVPIIRYPGGNFVSNYFWEDG VGPVEDRPRRLDLAWKSIEPNQVGINEFAKWCKKVNAEIM MAVNLGTRGISDACNLLEYCNHPGGSKYSDMRIKHGVKEP HNIKVWCLGNAMDGPWQVGHKTMDEYGRIAEETARAMKMI DPSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISLH QYYGNKENDTADFLAKSDDLDDFIRSVIATCDYIKAKKRS KKDIYLSFDEWNVWYHSNNEDANIMQNEPWRIAPPLLEDI YTFEDALLVGLMLITLMKHADRIKIACLAQLINVIAPIVT ERNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDTS KHEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSDV RGMKDYRLLEHIVLEHQDLKIRNSVNGEEVYPKNSDKSSF DDGILTSMLRRASWNVIRIG C:  ARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPGNS KSDEDGFRKDVIELVKELNVPIIRYPGGNFVSNYFWEDGV GPVEDRPRRLDLAWKSIEPNQVGINEFAKWCKKVNAEIMM AVNLGTRGISDACNLLEYCNHPGGSKYSDMRIKHGVKEPH NIKVWCLGNAMDGPWQVGHKTMDEYGRIAEETARAMKMID PSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISLHQ YYGNKENDTADFLAKSDDLDDFIRSVIATCDYIKAKKRSK KDIYLSFDEWNVWYHSNNEDANIMQNEPWRIAPPLLEDIY TFEDALLVGLMLITLMKHADRIKIACLAQLINVIAPIVTE RNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDTSK HEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSDVR GMKDYRLLEHIVLEHQDLKIRNSVNGEEVYPKNSDKSSFD DGILTSMLRRASWNVIRIG D:  ARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPGNS KSDEDGFRKDVIELVKELNVPIIRYPGGNFVSNYFWEDGV GPVEDRPRRLDLAWKSIEPNQVGINEFAKWCKKVNAEIMM AVNLGTRGISDACNLLEYCNHPGGSKYSDMRIKHGVKEPH NIKVWCLGNAMDGPWQVGHKTMDEYGRIAEETARAMKMID PSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISLHQ YYGNKENDTADFLAKSDDLDDFIRSVIATCDYIKAKKRSK KDIYLSFDEWNVWYHSNNEDANIMQNEPWRIAPPLLEDIY TFEDALLVGLMLITLMKHADRIKIACLAQLINVIAPIVTE RNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDTSK HEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSDVR GMKDYRLLEHIVLEHQDLKIRNSVNGEEVYPKNSDKSSFD DGITSMLRRASWNVIRIG E:  KARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPGN SKSDEDGFRKDVIELVKELNVPIIRYPGGNFVSNYFWEDG VGPVEDRPRRLDLAWKSIEPNQVGINEFAKWCKKVNAEIM MAVNLGTRGISDACNLLEYCNHPGGSKYSDMRIKHGVKEP HNIKVWCLGNAMDGPWQVGHKTMDEYGRIAEETARAMKMI DPSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISLH QYYGNKENDTADFLAKSDDLDDFIRSVIATCDYIKAKKRS KKDIYLSFDEWNVWYHSNNEDANIMQNEPWRIAPPLLEDI YTFEDALLVGLMLITLMKHADRIKIACLAQLINVIAPIVT ERNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDTS KHEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSDV RGMKDYRLLEHIVLEHQDLKIRNSVNGEEVYPKNSDKSSF ILTSMLRRASWNVIRIG F:  KARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPGN SKSDEDGFRKDVIELVKELNVPIIRYPGGNFVSNYFWEDG VGPVEDRPRRLDLAWKSIEPNQVGINEFAKWCKKVNAEIM MAVNLGTRGISDACNLLEYCNHPGGSKYSDMRIKHGVKEP HNIKVWCLGNAMDGPWQVGHKTMDEYGRIAEETARAMKMI DPSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISLH QYYGNKENDTADFLAKSDDLDDFIRSVIATCDYIKAKKRS KKDIYLSFDEWNVWYHSNNEDANIMQNEPWRIAPPLLEDI YTFEDALLVGLMLITLMKHADRIKIACLAQLINVIAPIVT ERNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDTS KHEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSDV RGMKDYRLLEHIVLEHQDLKIRNSVNGEEVYPKNSDKSSF DDGILTSMLRRASWNVIRIG Description Functional site 1) chain A residue 292 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:16336192 source Swiss-Prot : SWS_FT_FI2 2) chain B residue 292 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:16336192 source Swiss-Prot : SWS_FT_FI2 3) chain C residue 292 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:16336192 source Swiss-Prot : SWS_FT_FI2 4) chain D residue 292 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:16336192 source Swiss-Prot : SWS_FT_FI2 5) chain E residue 292 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:16336192 source Swiss-Prot : SWS_FT_FI2 6) chain F residue 292 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:16336192 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 296 type SITE sequence W description Important for substrate recognition => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 8) chain B residue 296 type SITE sequence W description Important for substrate recognition => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 9) chain C residue 296 type SITE sequence W description Important for substrate recognition => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 10) chain D residue 296 type SITE sequence W description Important for substrate recognition => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 11) chain E residue 296 type SITE sequence W description Important for substrate recognition => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 12) chain F residue 296 type SITE sequence W description Important for substrate recognition => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 13) chain A residue 352 type SITE sequence Q description Important for substrate recognition source Swiss-Prot : SWS_FT_FI6 14) chain B residue 352 type SITE sequence Q description Important for substrate recognition source Swiss-Prot : SWS_FT_FI6 15) chain C residue 352 type SITE sequence Q description Important for substrate recognition source Swiss-Prot : SWS_FT_FI6 16) chain D residue 352 type SITE sequence Q description Important for substrate recognition source Swiss-Prot : SWS_FT_FI6 17) chain E residue 352 type SITE sequence Q description Important for substrate recognition source Swiss-Prot : SWS_FT_FI6 18) chain F residue 352 type SITE sequence Q description Important for substrate recognition source Swiss-Prot : SWS_FT_FI6 19) chain A residue 27 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 20) chain C residue 72 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 21) chain C residue 244 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 22) chain C residue 292 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 23) chain D residue 27 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 24) chain D residue 72 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 25) chain D residue 244 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 26) chain D residue 292 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 27) chain E residue 27 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 28) chain E residue 72 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 29) chain E residue 244 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 30) chain A residue 72 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 31) chain E residue 292 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 32) chain F residue 27 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 33) chain F residue 72 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 34) chain F residue 244 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 35) chain F residue 292 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 36) chain A residue 244 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 37) chain A residue 292 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 38) chain B residue 27 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 39) chain B residue 72 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 40) chain B residue 244 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 41) chain B residue 292 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 42) chain C residue 27 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 43) chain A residue 172 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 44) chain E residue 352 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 45) chain F residue 172 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 46) chain F residue 352 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 47) chain A residue 352 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 48) chain B residue 172 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 49) chain B residue 352 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 50) chain C residue 172 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 51) chain C residue 352 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 52) chain D residue 172 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 53) chain D residue 352 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 54) chain E residue 172 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 173 type ACT_SITE sequence A description Proton donor/acceptor => ECO:0000305|PubMed:16336192 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 173 type ACT_SITE sequence A description Proton donor/acceptor => ECO:0000305|PubMed:16336192 source Swiss-Prot : SWS_FT_FI1 57) chain C residue 173 type ACT_SITE sequence A description Proton donor/acceptor => ECO:0000305|PubMed:16336192 source Swiss-Prot : SWS_FT_FI1 58) chain D residue 173 type ACT_SITE sequence A description Proton donor/acceptor => ECO:0000305|PubMed:16336192 source Swiss-Prot : SWS_FT_FI1 59) chain E residue 173 type ACT_SITE sequence A description Proton donor/acceptor => ECO:0000305|PubMed:16336192 source Swiss-Prot : SWS_FT_FI1 60) chain F residue 173 type ACT_SITE sequence A description Proton donor/acceptor => ECO:0000305|PubMed:16336192 source Swiss-Prot : SWS_FT_FI1

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