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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
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:20420880
ChainResidueDetails
ASER160
BSER160
CSER160
DSER160
ESER160
FSER160
GSER160
HSER160

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:20420880
ChainResidueDetails
ATYR175
BTYR175
CTYR175
DTYR175
ETYR175
FTYR175
GTYR175
HTYR175

site_idSWS_FT_FI3
Number of Residues8
DetailsACT_SITE: Lowers pKa of active site Tyr => ECO:0000305|PubMed:20420880
ChainResidueDetails
BLYS179
ALYS179
CLYS179
DLYS179
ELYS179
FLYS179
GLYS179
HLYS179

site_idSWS_FT_FI4
Number of Residues32
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O93868
ChainResidueDetails
DILE207
EASN108
ETYR175
ELYS179
EILE207
FASN108
FTYR175
FLYS179
FILE207
GASN108
GTYR175
GLYS179
GILE207
HASN108
HTYR175
HLYS179
HILE207
AASN108
CTYR175
CLYS179
CILE207
DASN108
DTYR175
DLYS179
ATYR175
ALYS179
AILE207
BASN108
BTYR175
BLYS179
BILE207
CASN108

site_idSWS_FT_FI5
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:L0E2Z4
ChainResidueDetails
ALYS141
ETHR209
FLYS141
FTHR209
GLYS141
GTHR209
HLYS141
HTHR209
ATHR209
BLYS141
BTHR209
CLYS141
CTHR209
DLYS141
DTHR209
ELYS141

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PDB entries from 2024-06-12

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