6BJP

Apo form of the E124S mutant of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0019285	biological_process	glycine betaine biosynthetic process from choline
A	0046872	molecular_function	metal ion binding
B	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0019285	biological_process	glycine betaine biosynthetic process from choline
B	0046872	molecular_function	metal ion binding
C	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0019285	biological_process	glycine betaine biosynthetic process from choline
C	0046872	molecular_function	metal ion binding
D	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0019285	biological_process	glycine betaine biosynthetic process from choline
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue K A 501

Chain	Residue
A	THR26
A	ILE27
A	ASP93
A	VAL180
A	HOH690

---

site_id	AC2
Number of Residues	9
Details	binding site for residue GOL A 502

Chain	Residue
C	GLU5
C	GLU6
C	GLN7
C	LYS8
C	TYR15
A	LEU307
A	LEU352
A	CYS353
A	HOH732

---

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 503

Chain	Residue
A	GLN311
C	PHE4
C	GLN7
C	LYS187

---

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL A 504

Chain	Residue
A	TYR115
A	ALA449
A	LYS457
A	GLN458
A	SER459
A	GLY460
A	VAL461
A	HOH707
A	HOH709

---

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 505

Chain	Residue
A	GLU482
D	ARG269
D	ASN442

---

site_id	AC6
Number of Residues	2
Details	binding site for residue EDO A 506

Chain	Residue
A	GLN7
A	LYS187

---

site_id	AC7
Number of Residues	1
Details	binding site for residue EDO A 507

Chain	Residue
A	HOH681

---

site_id	AC8
Number of Residues	5
Details	binding site for residue K B 501

Chain	Residue
B	THR26
B	ILE27
B	ASP93
B	VAL180
B	HOH635

---

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO B 502

Chain	Residue
B	GLY339
B	TYR340
B	GLU386
B	HOH681
B	HOH683

---

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO B 503

Chain	Residue
B	TYR116
B	TRP161
B	PRO165
B	ALA449
B	THR469

---

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO B 504

Chain	Residue
B	GLN7
B	LYS187

---

site_id	AD3
Number of Residues	2
Details	binding site for residue EDO B 505

Chain	Residue
B	GLU387
B	HOH715

---

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO B 506

Chain	Residue
B	GLY445
B	GLY455
B	TYR456

---

site_id	AD5
Number of Residues	5
Details	binding site for residue K C 501

Chain	Residue
C	THR26
C	ILE27
C	ASP93
C	VAL180
C	HOH723

---

site_id	AD6
Number of Residues	5
Details	binding site for residue K D 501

Chain	Residue
D	THR26
D	ILE27
D	ASP93
D	VAL180
D	HOH643

---

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfSSGQVCTNGT

Chain	Residue	Details
A	PHE279-THR290
C	PHE279-THR290

---

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGKSP

Chain	Residue	Details
A	MET251-PRO258
C	MET251-PRO258

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19013472","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21732915","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21732915","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WOX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"21732915","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WOX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19013472","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---