1PIW

APO AND HOLO STRUCTURES OF AN NADP(H)-DEPENDENT CINNAMYL ALCOHOL DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005575	cellular_component	cellular_component
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006066	biological_process	alcohol metabolic process
A	0006081	biological_process	aldehyde metabolic process
A	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
A	0008270	molecular_function	zinc ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0033833	molecular_function	hydroxymethylfurfural reductase (NADH) activity
A	0033845	molecular_function	hydroxymethylfurfural reductase (NADPH) activity
A	0033859	biological_process	furaldehyde metabolic process
A	0045551	molecular_function	cinnamyl-alcohol dehydrogenase activity
A	0046872	molecular_function	metal ion binding
A	0052675	molecular_function	3-methylbutanal reductase (NADPH) activity
B	0005575	cellular_component	cellular_component
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0006066	biological_process	alcohol metabolic process
B	0006081	biological_process	aldehyde metabolic process
B	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
B	0008270	molecular_function	zinc ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0033833	molecular_function	hydroxymethylfurfural reductase (NADH) activity
B	0033845	molecular_function	hydroxymethylfurfural reductase (NADPH) activity
B	0033859	biological_process	furaldehyde metabolic process
B	0045551	molecular_function	cinnamyl-alcohol dehydrogenase activity
B	0046872	molecular_function	metal ion binding
B	0052675	molecular_function	3-methylbutanal reductase (NADPH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1501

Chain	Residue
A	CYS100
A	CYS103
A	CYS106
A	CYS114

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 1502

Chain	Residue
A	CYS46
A	SER48
A	HIS68
A	CYS163
A	NAP4292

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 1501

Chain	Residue
B	SER99
B	CYS100
B	CYS103
B	CYS106
B	CYS114

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 1502

Chain	Residue
B	CYS46
B	SER48
B	HIS68
B	CYS163
B	NAP4293

---

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAP A 4292

Chain	Residue
A	GLY47
A	SER48
A	HIS51
A	THR167
A	GLY187
A	LEU188
A	GLY189
A	GLY190
A	ILE191
A	SER210
A	ARG211
A	LYS215
A	ALA251
A	SER252
A	SER253
A	THR255
A	ASP256
A	ILE275
A	ILE277
A	TYR298
A	SER299
A	ALA300
A	LEU301
A	ARG348
A	ZN1502

---

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAP B 4293

Chain	Residue
B	GLY47
B	CYS163
B	THR167
B	GLY187
B	LEU188
B	GLY189
B	GLY190
B	ILE191
B	SER210
B	ARG211
B	LYS215
B	CYS250
B	ALA251
B	SER252
B	ILE275
B	ILE277
B	SER299
B	ALA300
B	LEU301
B	ARG348
B	ZN1502

---

Functional Information from PROSITE/UniProt

site_id	PS00059
Number of Residues	15
Details	ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiVGKvvklGpkS

Chain	Residue	Details
A	GLY67-SER81

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PS0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PIW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PS0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
A	TRP57

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
B	TRP57

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
A	SER48
A	HIS51

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
B	SER48
B	HIS51

---