9LDK

The complex structure of Escherichia coli AdhE (compact conformation)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006115	biological_process	ethanol biosynthetic process
A	0006979	biological_process	response to oxidative stress
A	0008198	molecular_function	ferrous iron binding
A	0008774	molecular_function	acetaldehyde dehydrogenase (acetylating) activity
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0019664	biological_process	mixed acid fermentation
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051260	biological_process	protein homooligomerization
A	0120542	molecular_function	ethanol dehydrogenase (NAD+) activity
B	0003824	molecular_function	catalytic activity
B	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006115	biological_process	ethanol biosynthetic process
B	0006979	biological_process	response to oxidative stress
B	0008198	molecular_function	ferrous iron binding
B	0008774	molecular_function	acetaldehyde dehydrogenase (acetylating) activity
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0019664	biological_process	mixed acid fermentation
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051260	biological_process	protein homooligomerization
B	0120542	molecular_function	ethanol dehydrogenase (NAD+) activity
C	0003824	molecular_function	catalytic activity
C	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0006115	biological_process	ethanol biosynthetic process
C	0006979	biological_process	response to oxidative stress
C	0008198	molecular_function	ferrous iron binding
C	0008774	molecular_function	acetaldehyde dehydrogenase (acetylating) activity
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0019664	biological_process	mixed acid fermentation
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0051260	biological_process	protein homooligomerization
C	0120542	molecular_function	ethanol dehydrogenase (NAD+) activity
F	0003824	molecular_function	catalytic activity
F	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
F	0005515	molecular_function	protein binding
F	0005829	cellular_component	cytosol
F	0006115	biological_process	ethanol biosynthetic process
F	0006979	biological_process	response to oxidative stress
F	0008198	molecular_function	ferrous iron binding
F	0008774	molecular_function	acetaldehyde dehydrogenase (acetylating) activity
F	0016020	cellular_component	membrane
F	0016491	molecular_function	oxidoreductase activity
F	0019664	biological_process	mixed acid fermentation
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0051260	biological_process	protein homooligomerization
F	0120542	molecular_function	ethanol dehydrogenase (NAD+) activity

Functional Information from PROSITE/UniProt

site_id	PS00060
Number of Residues	21
Details	ADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. GvCHsmAHkLGSqfhIpHGlA

Chain	Residue	Details
A	GLY720-ALA740

---

site_id	PS00913
Number of Residues	29
Details	ADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. AIvDanlvmdmPkslcAfGglDAVthamE

Chain	Residue	Details
A	ALA632-GLU660

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Region: {"description":"Linker","evidences":[{"source":"PubMed","id":"31586059","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q9HTJ1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	50
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32523125","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7BVP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32188856","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32523125","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6TQH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TQM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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