eF-site ID 4cyj-ABCDEF PDB Code 4cyj Chain A, B, C, D, E, F click to enlarge Title Chaetomium thermophilum Pan2:Pan3 complex Classification TRANSFERASE Compound PAB-DEPENDENT POLY(A)-SPECIFIC RIBONUCLEASE SUBUNIT PAN3-LIKE PROTEIN Source Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (G0SAK8_CHATD) Sequence A:  ELQPWQRATYDFFMPQNLREDLQKKQFATLQVIPNSGLPQ LEHWHSLVPLDTSNRKNTSCFGYPSWVYKAQNSRNGRHYA LRRLEGYRLTNEKAILNVMKDWKKIKNASIVTIHEVFTTR EFGDSSLIFAYDFHPLSKTLQEHHFQPPAVPENTIWGYIC QIANALKTIHSNRLAARCLEPSKIILTDINRIRLSACAIL DVVQFGMNSRSVVELQQEDFVKFGKLILSLATGTLPAHLN NIPAALETLGNKYSANLKSAVNWLLDTSSGETKTIEHFMT GIASQMTTFFDLALQDNDEKLFHLAREVENGRIARSLMKL LTILERGDRYQLKLFRDYVFHRVDADGKPNLSIGHMLTCM SKLEAGVDENILLTSRDNETVFVLSYRELRQMYDRAFNEL VKA B:  ELQPWQRATYDFFMPQNLREDLQKKQFATLQVIPNSGLPQ LEHWHSLVPLDTSSCFGYPSWVYKAQNSRNGRHYALRRLE GYRLTNEKAILNVMKDWKKIKNASIVTIHEVFTTREFGDS SLIFAYDFHPLSKTLQEHHFQPYRPPPAVPENTIWGYICQ IANALKTIHSNRLAARCLEPSKIILTDINRIRLSACAILD VVQFGMNSRSVVELQQEDFVKFGKLILSLATGTLPAHLNN IPAALETLGNKYSANLKSAVNWLLDTSSGETKTIEHFMTG IASQMTTFFDLALQDNDEKLFHLAREVENGRIARSLMKLL TILERGDVPSWSETGDRYQLKLFRDYVFHRVDADGKPNLS IGHMLTCMSKLEAGVDENILLTSRDNETVFVLSYRELRQM YDRAFNELVKAS C:  PWQRATYDFFMPQNLREDLQKKQFATLQVIPNSGLPQLEH WHSLVPLDTSNRKNTSCFGYPSWVYKAQNSRNGRHYALRR LEGYRLTNEKAILNVMKDWKKIKNASIVTIHEVFTTREFG DSSLIFAYDFHPLSKTLQEHHFQPIPAVPENTIWGYICQI ANALKTIHSNRLAARCLEPSKIILTDINRIRLSACAILDV VQFGMNSRSVVELQQEDFVKFGKLILSLATGTLPAHLNNI PAALETLGNKYSANLKSAVNWLLDTSSGETKTIEHFMTGI ASQMTTFFDLALQDNDEKLFHLAREVENGRIARSLMKLLT ILERGGDRYQLKLFRDYVFHRVDADGKPNLSIGHMLTCMS KLEAGVDENILLTSRDNETVFVLSYRELRQMYDRAFNELV KASK D:  ELQPWQRATYDFFMPQNLREDLQKKQFATLQVIPNSGLPQ LEHWHSLVPLDTSTSCFGYPSWVYKAQNSRNGRHYALRRL EGYRLTNEKAILNVMKDWKKIKNASIVTIHEVFTTREFGD SSLIFAYDFHPLSKTLQEHHFQPPPPAVPENTIWGYICQI ANALKTIHSNRLAARCLEPSKIILTDINRIRLSACAILDV VQFGMNSRSVVELQQEDFVKFGKLILSLATGTLPAHLNNI PAALETLGNKYSANLKSAVNWLLDTSSGETKTIEHFMTGI ASQMTTFFDLALQDNDEKLFHLAREVENGRIARSLMKLLT ILERGDVPSWSETGDRYQLKLFRDYVFHRVDADGKPNLSI GHMLTCMSKLEAGVDENILLTSRDNETVFVLSYRELRQMY DRAFNELVKAS E:  PLFSAWPADIISDVGAPPLQLEPSFVATLKQAEWGLYGKN TRNVRRNQVEDT F:  PLFSAWPADIISDVGAPPLQLEPSFVATLKQAEWGLYGKN TRNVRRNQVEDTRN Description (1)  PAB-DEPENDENT POLY(A)-SPECIFIC RIBONUCLEASE SUBUNIT PAN3-LIKE PROTEIN, PAN2 Functional site 1) chain A residue 256 type sequence L description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 2) chain A residue 263 type sequence N description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 3) chain A residue 273 type sequence V description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 4) chain A residue 286 type sequence A description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 5) chain A residue 288 type sequence R description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 6) chain A residue 317 type sequence V description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 7) chain A residue 338 type sequence D description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 8) chain A residue 339 type sequence F description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 9) chain A residue 340 type sequence H description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 10) chain A residue 343 type sequence S description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 11) chain A residue 344 type sequence K description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 12) chain A residue 348 type sequence E description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 13) chain A residue 397 type sequence S description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 14) chain A residue 398 type sequence K description BINDING SITE FOR RESIDUE ATP A 900 source : AC1 15) chain A residue 257 type sequence D description BINDING SITE FOR RESIDUE MG A 1000 source : AC2 16) chain A residue 271 type sequence S description BINDING SITE FOR RESIDUE MG A 1000 source : AC2 17) chain B residue 265 type sequence S description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 18) chain B residue 288 type sequence R description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 19) chain B residue 317 type sequence V description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 20) chain B residue 338 type sequence D description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 21) chain B residue 340 type sequence H description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 22) chain B residue 343 type sequence S description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 23) chain B residue 347 type sequence Q description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 24) chain B residue 348 type sequence E description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 25) chain B residue 397 type sequence S description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 26) chain B residue 398 type sequence K description BINDING SITE FOR RESIDUE ATP B 900 source : AC3 27) chain B residue 257 type sequence D description BINDING SITE FOR RESIDUE MG B 1000 source : AC4 28) chain B residue 288 type sequence R description BINDING SITE FOR RESIDUE MG B 1000 source : AC4 29) chain C residue 257 type sequence D description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 30) chain C residue 263 type sequence N description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 31) chain C residue 273 type sequence V description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 32) chain C residue 286 type sequence A description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 33) chain C residue 288 type sequence R description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 34) chain C residue 317 type sequence V description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 35) chain C residue 338 type sequence D description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 36) chain C residue 340 type sequence H description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 37) chain C residue 343 type sequence S description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 38) chain C residue 344 type sequence K description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 39) chain C residue 348 type sequence E description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 40) chain C residue 397 type sequence S description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 41) chain C residue 398 type sequence K description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 42) chain C residue 400 type sequence I description BINDING SITE FOR RESIDUE ATP C 900 source : AC5 43) chain C residue 257 type sequence D description BINDING SITE FOR RESIDUE MG C 1000 source : AC6 44) chain D residue 257 type sequence D description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 45) chain D residue 264 type sequence T description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 46) chain D residue 271 type sequence S description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 47) chain D residue 288 type sequence R description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 48) chain D residue 317 type sequence V description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 49) chain D residue 338 type sequence D description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 50) chain D residue 339 type sequence F description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 51) chain D residue 340 type sequence H description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 52) chain D residue 343 type sequence S description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 53) chain D residue 344 type sequence K description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 54) chain D residue 348 type sequence E description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 55) chain D residue 397 type sequence S description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 56) chain D residue 398 type sequence K description BINDING SITE FOR RESIDUE ATP D 900 source : AC7 57) chain D residue 257 type sequence D description BINDING SITE FOR RESIDUE MG D 1000 source : AC8 58) chain D residue 271 type sequence S description BINDING SITE FOR RESIDUE MG D 1000 source : AC8 59) chain A residue 263 type BINDING sequence N description BINDING => ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI1 60) chain C residue 263 type BINDING sequence N description BINDING => ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 288 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 62) chain D residue 288 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 63) chain D residue 338 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 64) chain D residue 397 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 65) chain A residue 338 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 66) chain A residue 397 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 67) chain B residue 288 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 338 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 69) chain B residue 397 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 70) chain C residue 288 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 71) chain C residue 338 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2 72) chain C residue 397 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509 source Swiss-Prot : SWS_FT_FI2

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