3GDG

Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016491	molecular_function	oxidoreductase activity
A	0019594	biological_process	mannitol metabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
A	0050661	molecular_function	NADP binding
A	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
A	0051289	biological_process	protein homotetramerization
B	0016491	molecular_function	oxidoreductase activity
B	0019594	biological_process	mannitol metabolic process
B	0042803	molecular_function	protein homodimerization activity
B	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
B	0050661	molecular_function	NADP binding
B	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
B	0051289	biological_process	protein homotetramerization
C	0016491	molecular_function	oxidoreductase activity
C	0019594	biological_process	mannitol metabolic process
C	0042803	molecular_function	protein homodimerization activity
C	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
C	0050661	molecular_function	NADP binding
C	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
C	0051289	biological_process	protein homotetramerization
D	0016491	molecular_function	oxidoreductase activity
D	0019594	biological_process	mannitol metabolic process
D	0042803	molecular_function	protein homodimerization activity
D	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
D	0050661	molecular_function	NADP binding
D	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1002

Chain	Residue
A	ARG267
A	HOH304
A	HOH419
D	ARG267
D	HOH269
D	HOH668

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 1001

Chain	Residue
B	HOH317
B	HOH327
C	ARG267
B	ARG267
B	HOH296
B	HOH298

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"L0E2Z4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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