2AGZ

Crystal structure of the carbinolamine intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. F222 form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016491	molecular_function	oxidoreductase activity
A	0030058	molecular_function	aliphatic amine dehydrogenase activity
A	0030059	molecular_function	aralkylamine dehydrogenase (azurin) activity
A	0042597	cellular_component	periplasmic space
B	0016491	molecular_function	oxidoreductase activity
B	0030058	molecular_function	aliphatic amine dehydrogenase activity
B	0030059	molecular_function	aralkylamine dehydrogenase (azurin) activity
B	0042597	cellular_component	periplasmic space
D	0009308	biological_process	amine metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
D	0030059	molecular_function	aralkylamine dehydrogenase (azurin) activity
D	0042597	cellular_component	periplasmic space
H	0009308	biological_process	amine metabolic process
H	0016491	molecular_function	oxidoreductase activity
H	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
H	0030059	molecular_function	aralkylamine dehydrogenase (azurin) activity
H	0042597	cellular_component	periplasmic space

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN H 300

Chain	Residue
H	HIS114
H	HIS114
H	ASP121
H	ASP121

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS114
D	HIS114
D	ASP121
D	ASP121

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TSC D 190

Chain	Residue
B	GLY178
B	HOH885
D	ASP84
D	TRQ109
D	ASP128
D	VAL158
D	ASN159
D	TRP160
D	PHE169
D	THR172
B	LEU100

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TSC H 191

Chain	Residue
A	LEU100
A	GLY178
H	ASP84
H	TRQ109
H	ASP128
H	ASN156
H	VAL158
H	ASN159
H	TRP160
H	PHE169

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Tryptophylquinone 6'-substrate hemiaminal intermediate"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16614214","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17005560","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16614214","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17005560","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Tryptophylquinone","evidences":[{"source":"PubMed","id":"16614214","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17005560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17087503","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16614214","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17005560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17087503","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 2bbk

Chain	Residue	Details
D	THR172
D	ASP84
D	PHE169
D	TRP160
D	ASP128

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 2bbk

Chain	Residue	Details
H	THR172
H	ASP84
H	PHE169
H	TRP160
H	ASP128

---