eF-site ID 3gdg-ABCD PDB Code 3gdg 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 null (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 267 type sequence R description BINDING SITE FOR RESIDUE NA A 1002 source : AC1 2) chain D residue 267 type sequence R description BINDING SITE FOR RESIDUE NA A 1002 source : AC1 3) chain B residue 267 type sequence R description BINDING SITE FOR RESIDUE NA B 1001 source : AC2 4) chain C residue 267 type sequence R description BINDING SITE FOR RESIDUE NA B 1001 source : AC2 5) chain A residue 175 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 160 type ACT_SITE sequence S description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 7) chain B residue 175 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 8) chain C residue 160 type ACT_SITE sequence S description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 9) chain C residue 175 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 10) chain D residue 160 type ACT_SITE sequence S description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 11) chain D residue 175 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 160 type ACT_SITE sequence S description Proton donor => ECO:0000305|PubMed:20420880 source Swiss-Prot : SWS_FT_FI1 13) 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_FI2 14) 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_FI2 15) 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_FI2 16) 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_FI2 17) chain C residue 175 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 18) chain C residue 179 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 19) chain C residue 207 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 20) chain D residue 108 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 21) chain D residue 175 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 22) chain D residue 179 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 23) chain D residue 207 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 108 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 175 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 179 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 207 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 28) chain C residue 108 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 179 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 207 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 108 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 175 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:O93868 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 141 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 209 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 141 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 209 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI4 37) chain C residue 141 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI4 38) chain C residue 209 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI4 39) chain D residue 141 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI4 40) chain D residue 209 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:L0E2Z4 source Swiss-Prot : SWS_FT_FI4

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