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7KRG

Crystal Structure of Mannitol Dehydrogenase (ChMDH) from Cladosporium herbarum in complex with NADP+ and Na

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0019594biological_processmannitol metabolic process
A0042803molecular_functionprotein homodimerization activity
A0050085molecular_functionmannitol 2-dehydrogenase (NADP+) activity
A0050661molecular_functionNADP binding
A0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
A0051289biological_processprotein homotetramerization
B0016491molecular_functionoxidoreductase activity
B0019594biological_processmannitol metabolic process
B0042803molecular_functionprotein homodimerization activity
B0050085molecular_functionmannitol 2-dehydrogenase (NADP+) activity
B0050661molecular_functionNADP binding
B0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
B0051289biological_processprotein homotetramerization
C0016491molecular_functionoxidoreductase activity
C0019594biological_processmannitol metabolic process
C0042803molecular_functionprotein homodimerization activity
C0050085molecular_functionmannitol 2-dehydrogenase (NADP+) activity
C0050661molecular_functionNADP binding
C0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
C0051289biological_processprotein homotetramerization
D0016491molecular_functionoxidoreductase activity
D0019594biological_processmannitol metabolic process
D0042803molecular_functionprotein homodimerization activity
D0050085molecular_functionmannitol 2-dehydrogenase (NADP+) activity
D0050661molecular_functionNADP binding
D0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
D0051289biological_processprotein homotetramerization
E0016491molecular_functionoxidoreductase activity
E0019594biological_processmannitol metabolic process
E0042803molecular_functionprotein homodimerization activity
E0050085molecular_functionmannitol 2-dehydrogenase (NADP+) activity
E0050661molecular_functionNADP binding
E0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
E0051289biological_processprotein homotetramerization
F0016491molecular_functionoxidoreductase activity
F0019594biological_processmannitol metabolic process
F0042803molecular_functionprotein homodimerization activity
F0050085molecular_functionmannitol 2-dehydrogenase (NADP+) activity
F0050661molecular_functionNADP binding
F0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
F0051289biological_processprotein homotetramerization
G0016491molecular_functionoxidoreductase activity
G0019594biological_processmannitol metabolic process
G0042803molecular_functionprotein homodimerization activity
G0050085molecular_functionmannitol 2-dehydrogenase (NADP+) activity
G0050661molecular_functionNADP binding
G0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
G0051289biological_processprotein homotetramerization
H0016491molecular_functionoxidoreductase activity
H0019594biological_processmannitol metabolic process
H0042803molecular_functionprotein homodimerization activity
H0050085molecular_functionmannitol 2-dehydrogenase (NADP+) activity
H0050661molecular_functionNADP binding
H0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
H0051289biological_processprotein homotetramerization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsActive site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"L0E2Z4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-10-22

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