eF-site ID 3gdf-ABCD PDB Code 3gdf Chain A, B, C, D click to enlarge Title Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum. Classification OXIDOREDUCTASE Compound Probable NADP-dependent mannitol dehydrogenase Source Davidiella tassiana (Mycosphaerella tassiana) (Cladosporium herbarum) (MTDH_CLAHE) Sequence A:  MPGQQATKHESLLDQLSLKGKVVVVTGASGPKGMGIEAAR GCAEMGAAVAITYASRAQGAEENVKELEKTYGIKAKAYKC QVDSYESCEKLVKDVVADFGQIDAFIANAGATADSGILDG SVEAWNHVVQVDLNGTFHCAKAVGHHFKERGTGSLVITAS MSGHIANFPQEQTSYNVAKAGCIHMARSLANEWRDFARVN SISPGYIDTGLSDFVPKETQQLWHSMIPMGRDGLAKELKG AYVYFASDASTYTTGADLLIDGGYTTR B:  MPGQQATKHESLLDQLSLKGKVVVVTGASGPKGMGIEAAR GCAEMGAAVAITYASRAQGAEENVKELEKTYGIKAKAYKC QVDSYESCEKLVKDVVADFGQIDAFIANAGATADSGILDG SVEAWNHVVQVDLNGTFHCAKAVGHHFKERGTGSLVITAS MSGHIANFPQEQTSYNVAKAGCIHMARSLANEWRDFARVN SISPGYIDTGLSDFVPKETQQLWHSMIPMGRDGLAKELKG AYVYFASDASTYTTGADLLIDGGYTTR C:  MPGQQATKHESLLDQLSLKGKVVVVTGASGPKGMGIEAAR GCAEMGAAVAITYASRAQGAEENVKELEKTYGIKAKAYKC QVDSYESCEKLVKDVVADFGQIDAFIANAGATADSGILDG SVEAWNHVVQVDLNGTFHCAKAVGHHFKERGTGSLVITAS MSGHIANFPQEQTSYNVAKAGCIHMARSLANEWRDFARVN SISPGYIDTGLSDFVPKETQQLWHSMIPMGRDGLAKELKG AYVYFASDASTYTTGADLLIDGGYTTR D:  MPGQQATKHESLLDQLSLKGKVVVVTGASGPKGMGIEAAR GCAEMGAAVAITYASRAQGAEENVKELEKTYGIKAKAYKC QVDSYESCEKLVKDVVADFGQIDAFIANAGATADSGILDG SVEAWNHVVQVDLNGTFHCAKAVGHHFKERGTGSLVITAS MSGHIANFPQEQTSYNVAKAGCIHMARSLANEWRDFARVN SISPGYIDTGLSDFVPKETQQLWHSMIPMGRDGLAKELKG AYVYFASDASTYTTGADLLIDGGYTTR Description Functional site 1) chain A residue 123 type sequence E description BINDING SITE FOR RESIDUE ZN A 1003 source : AC1 2) chain A residue 127 type sequence H description BINDING SITE FOR RESIDUE ZN A 1003 source : AC1 3) chain D residue 86 type sequence E description BINDING SITE FOR RESIDUE ZN A 1003 source : AC1 4) chain D residue 89 type sequence E description BINDING SITE FOR RESIDUE ZN A 1003 source : AC1 5) chain A residue 267 type sequence R description BINDING SITE FOR RESIDUE ZN A 1004 source : AC2 6) chain D residue 267 type sequence R description BINDING SITE FOR RESIDUE ZN A 1004 source : AC2 7) chain B residue 267 type sequence R description BINDING SITE FOR RESIDUE ZN B 1001 source : AC3 8) chain C residue 267 type sequence R description BINDING SITE FOR RESIDUE ZN B 1001 source : AC3 9) chain B residue 123 type sequence E description BINDING SITE FOR RESIDUE ZN B 1002 source : AC4 10) chain B residue 127 type sequence H description BINDING SITE FOR RESIDUE ZN B 1002 source : AC4 11) chain C residue 86 type sequence E description BINDING SITE FOR RESIDUE ZN B 1002 source : AC4 12) chain C residue 89 type sequence E description BINDING SITE FOR RESIDUE ZN B 1002 source : AC4 13) chain A residue 160 type ACT_SITE sequence S description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 160 type ACT_SITE sequence S description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 160 type ACT_SITE sequence S description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 16) chain D residue 160 type ACT_SITE sequence S description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 175 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 175 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI2 19) chain C residue 175 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI2 20) chain D residue 175 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 179 type ACT_SITE sequence K description Lowers pKa of active site Tyr => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 179 type ACT_SITE sequence K description Lowers pKa of active site Tyr => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI3 23) chain C residue 179 type ACT_SITE sequence K description Lowers pKa of active site Tyr => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI3 24) chain D residue 179 type ACT_SITE sequence K description Lowers pKa of active site Tyr => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 108 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 26) chain C residue 175 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 27) chain C residue 179 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 28) chain C residue 207 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 29) chain D residue 108 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 30) chain D residue 175 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 31) chain D residue 179 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 32) chain D residue 207 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 175 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 179 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 207 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 108 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 175 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 179 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 39) chain B residue 207 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 40) chain C residue 108 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 141 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI5 42) chain A residue 209 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI5 43) chain B residue 141 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI5 44) chain B residue 209 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI5 45) chain C residue 141 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI5 46) chain C residue 209 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI5 47) chain D residue 141 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI5 48) chain D residue 209 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links