eF-site ID 1l7e-ABCD PDB Code 1l7e Chain A, B, C, D click to enlarge Title Crystal Structure of R. rubrum Transhydrogenase Domain I with Bound NADH Classification OXIDOREDUCTASE Compound nicotinamide nucleotide Transhydrogenase, subunit alpha 1 Source Rhodospirillum rubrum (PNTAA_RHORU) Sequence A:  MKIAIPKERRPGEDRVAISPEVVKKLVGLGFEVIVEQGAG VGASITDDALTAAGATIASTAAQALSQADVVWKVQRPMTA EEGTDEVALIKEGAVLMCHLGALTNRPVVEALTKRKITAY AMELMPRISRAQSMDILSSQSNLAGYRAVIDGAYEFARAF PMMMTAAGTVPPARVLVFGVGVAGLQAIATAKRLGAVVMA TDVRAATKEQVESLGGKFITVDDETAGGYAKEMGEEFRKK QAEAVLKELVKTDIAITTALIPGKPAPVLITEEMVTKMKP GSVIIDLAVEAGGNCPLSEPGKIVVKHGVKIVGHTNVPSR VAADASPLFAKNLLNFLTPHVDKDTKTLVMKLEDETVSGT CVTRDGAIVHPA B:  MKIAIPKERRPGEDRVAISPEVVKKLVGLGFEVIVEQGAG VGASITDDALTAAGATIASTAAQALSQADVVWKVQRPMTA EEGTDEVALIKEGAVLMCHLGALTNRPVVEALTKRKITAY AMELMPRISRAQSMDILSSQSNLAGYRAVIDGAYEFARAF PMMMTAAGTVPPARVLVFGVGVAGLQAIATAKRLGAVVMA TDVRAATKEQVESLGGKFITVRKKQAEAVLKELVKTDIAI TTALIPGKPAPVLITEEMVTKMKPGSVIIDLAVEAGGNCP LSEPGKIVVKHGVKIVGHTNVPSRVAADASPLFAKNLLNF LTPHVDKDTKTLVMKLEDETVSGTCVTRDGAIVHPAL C:  MKIAIPKERRPGEDRVAISPEVVKKLVGLGFEVIVEQGAG VGASITDDALTAAGATIASTAAQALSQADVVWKVQRPMTA EEGTDEVALIKEGAVLMCHLGALTNRPVVEALTKRKITAY AMELMPRISRAQSMDILSSQSNLAGYRAVIDGAYEFARAF PMMMTAAGTVPPARVLVFGVGVAGLQAIATAKRLGAVVMA TDVRAATKEQVESLGGKFIKQAEAVLKELVKTDIAITTAL IPGKPAPVLITEEMVTKMKPGSVIIDLAVEAGGNCPLSEP GKIVVKHGVKIVGHTNVPSRVAADASPLFAKNLLNFLTPH VDKDTKTLVMKLEDETVSGTCVTRDGAIVHPAL D:  MKIAIPKERRPGEDRVAISPEVVKKLVGLGFEVIVEQGAG VGASITDDALTAAGATIASTAAQALSQADVVWKVQRPMTA EEGTDEVALIKEGAVLMCHLGALTNRPVVEALTKRKITAY AMELMPRISRAQSMDILSSQSNLAGYRAVIDGAYEFARAF PMMMTAAGTVPPARVLVFGVGVAGLQAIATAKRLGAVVMA TDVRAATKEQVESLGGKFITVDGGYAKEMGEEFRKKQAEA VLKELVKTDIAITTALIPGKPAPVLITEEMVTKMKPGSVI IDLAVEAGGNCPLSEPGKIVVKHGVKIVGHTNVPSRVAAD ASPLFAKNLLNFLTPHVDKDTKTLVMKLEDETVSGTCVTR DGAIVHP Description Functional site 1) chain A residue 127 type sequence R description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 2) chain A residue 128 type sequence I description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 3) chain A residue 129 type sequence S description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 4) chain A residue 132 type sequence Q description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 5) chain A residue 135 type sequence D description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 6) chain A residue 138 type sequence S description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 7) chain A residue 179 type sequence G description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 8) chain A residue 180 type sequence V description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 9) chain A residue 181 type sequence G description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 10) chain A residue 182 type sequence V description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 11) chain A residue 202 type sequence D description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 12) chain A residue 203 type sequence V description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 13) chain A residue 204 type sequence R description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 14) chain A residue 236 type sequence A description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 15) chain A residue 247 type sequence Q description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 16) chain A residue 264 type sequence T description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 17) chain A residue 265 type sequence A description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 18) chain A residue 266 type sequence L description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 19) chain A residue 273 type sequence P description BINDING SITE FOR RESIDUE NAI A 701 source : AC1 20) chain D residue 1327 type sequence R description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 21) chain D residue 1328 type sequence I description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 22) chain D residue 1332 type sequence Q description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 23) chain D residue 1335 type sequence D description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 24) chain D residue 1338 type sequence S description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 25) chain D residue 1379 type sequence G description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 26) chain D residue 1380 type sequence V description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 27) chain D residue 1381 type sequence G description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 28) chain D residue 1382 type sequence V description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 29) chain D residue 1402 type sequence D description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 30) chain D residue 1404 type sequence R description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 31) chain D residue 1436 type sequence A description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 32) chain D residue 1447 type sequence Q description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 33) chain D residue 1464 type sequence T description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 34) chain D residue 1465 type sequence A description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 35) chain D residue 1466 type sequence L description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 36) chain D residue 1473 type sequence P description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 37) chain D residue 1475 type sequence L description BINDING SITE FOR RESIDUE NAI D 702 source : AC2 38) chain A residue 127 type catalytic sequence R description 116 source MCSA : MCSA1 39) chain A residue 132 type catalytic sequence Q description 116 source MCSA : MCSA1 40) chain A residue 135 type catalytic sequence D description 116 source MCSA : MCSA1 41) chain A residue 138 type catalytic sequence S description 116 source MCSA : MCSA1 42) chain A residue 235 type catalytic sequence Y description 116 source MCSA : MCSA1 43) chain B residue 527 type catalytic sequence R description 116 source MCSA : MCSA2 44) chain B residue 532 type catalytic sequence Q description 116 source MCSA : MCSA2 45) chain B residue 535 type catalytic sequence D description 116 source MCSA : MCSA2 46) chain B residue 538 type catalytic sequence S description 116 source MCSA : MCSA2 47) chain C residue 927 type catalytic sequence R description 116 source MCSA : MCSA3 48) chain C residue 932 type catalytic sequence Q description 116 source MCSA : MCSA3 49) chain C residue 935 type catalytic sequence D description 116 source MCSA : MCSA3 50) chain C residue 938 type catalytic sequence S description 116 source MCSA : MCSA3 51) chain D residue 1327 type catalytic sequence R description 116 source MCSA : MCSA4 52) chain D residue 1332 type catalytic sequence Q description 116 source MCSA : MCSA4 53) chain D residue 1335 type catalytic sequence D description 116 source MCSA : MCSA4 54) chain D residue 1338 type catalytic sequence S description 116 source MCSA : MCSA4 55) chain D residue 1435 type catalytic sequence Y description 116 source MCSA : MCSA4 56) chain A residue 4-30 type prosite sequence AIPKERRPGEDRVAISPEVVKKLVGLG description ALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. AIPkErrpGEd..RVAiSPeVVkkLvGlG source prosite : PS00836 57) chain A residue 177-202 type prosite sequence VFGVGVAGLQAIATAKRLGAVVMATD description ALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VFGVGvAGlqAiatAkRLGAvVmatD source prosite : PS00837 58) chain A residue 132 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 59) chain D residue 1332 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 60) chain D residue 1402 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 61) chain D residue 1434 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 62) chain A residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 63) chain A residue 180 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 64) chain A residue 247 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 65) chain A residue 266 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 527 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 67) chain B residue 580 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 647 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 202 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 666 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 71) chain C residue 927 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 72) chain C residue 980 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 73) chain C residue 1047 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 74) chain C residue 1066 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 75) chain D residue 1327 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 76) chain D residue 1380 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 77) chain D residue 1447 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 78) chain D residue 1466 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 79) chain A residue 234 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 80) chain B residue 532 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 81) chain B residue 602 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 82) chain C residue 932 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 83) chain C residue 1002 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 source Swiss-Prot : SWS_FT_FI1 84) chain A residue 182 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 85) chain B residue 582 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 86) chain C residue 982 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 87) chain D residue 1382 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2

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