eF-site ID 1bxz-ABCD PDB Code 1bxz Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURE OF A THERMOPHILIC ALCOHOL DEHYDROGENASE SUBSTRATE COMPLEX FROM THERMOANAEROBACTER BROCKII Classification OXIDOREDUCTASE Compound NADP-DEPENDENT ALCOHOL DEHYDROGENASE Source null (ADH_THEBR) Sequence A:  MKGFAMLSIGKVGWIEKEKPAPGPFDAIVRPLAVAPCTSD IHTVFEGAIGERHNMILGHEAVGEVVEVGSEVKDFKPGDR VVVPAITPDWRTSEVQRGYHQHSGGMLAGWKFSNVKDGVF GEFFHVNDADMNLAHLPKEIPLEAAVMIPDMMTTGFHGAE LADIELGATVAVLGIGPVGLMAVAGAKLRGAGRIIAVGSR PVCVDAAKYYGATDIVNYKDGPIESQIMNLTEGKGVDAAI IAGGNADIMATAVKIVKPGGTIANVNYFGEGEVLPVPRLE WGCGMAHKTIKGGLCPGGRLRMERLIDLVFYKRVDPSKLV THVFRGFDNIEKAFMLMKDKPKDLIKPVVILA B:  MKGFAMLSIGKVGWIEKEKPAPGPFDAIVRPLAVAPCTSD IHTVFEGAIGERHNMILGHEAVGEVVEVGSEVKDFKPGDR VVVPAITPDWRTSEVQRGYHQHSGGMLAGWKFSNVKDGVF GEFFHVNDADMNLAHLPKEIPLEAAVMIPDMMTTGFHGAE LADIELGATVAVLGIGPVGLMAVAGAKLRGAGRIIAVGSR PVCVDAAKYYGATDIVNYKDGPIESQIMNLTEGKGVDAAI IAGGNADIMATAVKIVKPGGTIANVNYFGEGEVLPVPRLE WGCGMAHKTIKGGLCPGGRLRMERLIDLVFYKRVDPSKLV THVFRGFDNIEKAFMLMKDKPKDLIKPVVILA C:  MKGFAMLSIGKVGWIEKEKPAPGPFDAIVRPLAVAPCTSD IHTVFEGAIGERHNMILGHEAVGEVVEVGSEVKDFKPGDR VVVPAITPDWRTSEVQRGYHQHSGGMLAGWKFSNVKDGVF GEFFHVNDADMNLAHLPKEIPLEAAVMIPDMMTTGFHGAE LADIELGATVAVLGIGPVGLMAVAGAKLRGAGRIIAVGSR PVCVDAAKYYGATDIVNYKDGPIESQIMNLTEGKGVDAAI IAGGNADIMATAVKIVKPGGTIANVNYFGEGEVLPVPRLE WGCGMAHKTIKGGLCPGGRLRMERLIDLVFYKRVDPSKLV THVFRGFDNIEKAFMLMKDKPKDLIKPVVILA D:  MKGFAMLSIGKVGWIEKEKPAPGPFDAIVRPLAVAPCTSD IHTVFEGAIGERHNMILGHEAVGEVVEVGSEVKDFKPGDR VVVPAITPDWRTSEVQRGYHQHSGGMLAGWKFSNVKDGVF GEFFHVNDADMNLAHLPKEIPLEAAVMIPDMMTTGFHGAE LADIELGATVAVLGIGPVGLMAVAGAKLRGAGRIIAVGSR PVCVDAAKYYGATDIVNYKDGPIESQIMNLTEGKGVDAAI IAGGNADIMATAVKIVKPGGTIANVNYFGEGEVLPVPRLE WGCGMAHKTIKGGLCPGGRLRMERLIDLVFYKRVDPSKLV THVFRGFDNIEKAFMLMKDKPKDLIKPVVILA Description Functional site 1) chain A residue 37 type sequence C description BINDING SITE FOR RESIDUE ZN A 354 source : AC1 2) chain A residue 38 type sequence T description BINDING SITE FOR RESIDUE ZN A 354 source : AC1 3) chain A residue 346 type sequence K description BINDING SITE FOR RESIDUE ZN A 354 source : AC1 4) chain A residue 193 type sequence R description BINDING SITE FOR RESIDUE CL A 355 source : AC2 5) chain A residue 234 type sequence K description BINDING SITE FOR RESIDUE CL A 355 source : AC2 6) chain A residue 307 type sequence D description BINDING SITE FOR RESIDUE MG A 356 source : AC3 7) chain B residue 37 type sequence C description BINDING SITE FOR RESIDUE ZN B 354 source : AC4 8) chain B residue 38 type sequence T description BINDING SITE FOR RESIDUE ZN B 354 source : AC4 9) chain B residue 60 type sequence E description BINDING SITE FOR RESIDUE ZN B 354 source : AC4 10) chain B residue 346 type sequence K description BINDING SITE FOR RESIDUE ZN B 354 source : AC4 11) chain B residue 193 type sequence R description BINDING SITE FOR RESIDUE CL B 355 source : AC5 12) chain B residue 234 type sequence K description BINDING SITE FOR RESIDUE CL B 355 source : AC5 13) chain B residue 307 type sequence D description BINDING SITE FOR RESIDUE MG B 356 source : AC6 14) chain C residue 36 type sequence P description BINDING SITE FOR RESIDUE ZN C 354 source : AC7 15) chain C residue 37 type sequence C description BINDING SITE FOR RESIDUE ZN C 354 source : AC7 16) chain C residue 38 type sequence T description BINDING SITE FOR RESIDUE ZN C 354 source : AC7 17) chain C residue 60 type sequence E description BINDING SITE FOR RESIDUE ZN C 354 source : AC7 18) chain C residue 346 type sequence K description BINDING SITE FOR RESIDUE ZN C 354 source : AC7 19) chain C residue 193 type sequence R description BINDING SITE FOR RESIDUE CL C 355 source : AC8 20) chain C residue 307 type sequence D description BINDING SITE FOR RESIDUE MG C 356 source : AC9 21) chain D residue 37 type sequence C description BINDING SITE FOR RESIDUE ZN D 354 source : BC1 22) chain D residue 38 type sequence T description BINDING SITE FOR RESIDUE ZN D 354 source : BC1 23) chain D residue 193 type sequence R description BINDING SITE FOR RESIDUE CL D 355 source : BC2 24) chain D residue 307 type sequence D description BINDING SITE FOR RESIDUE MG D 356 source : BC3 25) chain A residue 150 type sequence D description BINDING SITE FOR RESIDUE SBT A 353 source : BC4 26) chain B residue 59 type sequence H description BINDING SITE FOR RESIDUE SBT B 353 source : BC5 27) chain B residue 150 type sequence D description BINDING SITE FOR RESIDUE SBT B 353 source : BC5 28) chain C residue 150 type sequence D description BINDING SITE FOR RESIDUE SBT C 353 source : BC6 29) chain D residue 59 type sequence H description BINDING SITE FOR RESIDUE SBT D 353 source : BC7 30) chain D residue 150 type sequence D description BINDING SITE FOR RESIDUE SBT D 353 source : BC7 31) chain A residue 37 type BINDING sequence C description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 59 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 150 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 37 type BINDING sequence C description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 59 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 150 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 37) chain C residue 37 type BINDING sequence C description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 59 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 150 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 40) chain D residue 37 type BINDING sequence C description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 59 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 42) chain D residue 150 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 265 type BINDING sequence V description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 340 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 175 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 198 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 265 type BINDING sequence V description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 340 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 50) chain C residue 175 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 51) chain C residue 198 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 52) chain C residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 53) chain C residue 265 type BINDING sequence V description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 54) chain C residue 340 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 55) chain D residue 175 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 56) chain D residue 198 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 57) chain D residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 58) chain D residue 265 type BINDING sequence V description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 59) chain D residue 340 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 175 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 198 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 62) chain A residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9836873 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 58-72 type prosite sequence GHEAVGEVVEVGSEV description ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaVGEvvevGseV source prosite : PS00059

Display surface Download Links