3OA2

Crystal structure of the WlbA (WbpB) dehydrogenase from Pseudomonas aeruginosa in complex with NAD at 1.5 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000271	biological_process	polysaccharide biosynthetic process
A	0003954	molecular_function	NADH dehydrogenase activity
A	0004617	molecular_function	phosphoglycerate dehydrogenase activity
A	0006065	biological_process	UDP-glucuronate biosynthetic process
A	0009103	biological_process	lipopolysaccharide biosynthetic process
A	0009243	biological_process	O antigen biosynthetic process
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	0051262	biological_process	protein tetramerization
A	0070403	molecular_function	NAD+ binding
A	0070404	molecular_function	NADH binding
A	0071555	biological_process	cell wall organization
B	0000166	molecular_function	nucleotide binding
B	0000271	biological_process	polysaccharide biosynthetic process
B	0003954	molecular_function	NADH dehydrogenase activity
B	0004617	molecular_function	phosphoglycerate dehydrogenase activity
B	0006065	biological_process	UDP-glucuronate biosynthetic process
B	0009103	biological_process	lipopolysaccharide biosynthetic process
B	0009243	biological_process	O antigen biosynthetic process
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	0051262	biological_process	protein tetramerization
B	0070403	molecular_function	NAD+ binding
B	0070404	molecular_function	NADH binding
B	0071555	biological_process	cell wall organization
C	0000166	molecular_function	nucleotide binding
C	0000271	biological_process	polysaccharide biosynthetic process
C	0003954	molecular_function	NADH dehydrogenase activity
C	0004617	molecular_function	phosphoglycerate dehydrogenase activity
C	0006065	biological_process	UDP-glucuronate biosynthetic process
C	0009103	biological_process	lipopolysaccharide biosynthetic process
C	0009243	biological_process	O antigen biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0051262	biological_process	protein tetramerization
C	0070403	molecular_function	NAD+ binding
C	0070404	molecular_function	NADH binding
C	0071555	biological_process	cell wall organization
D	0000166	molecular_function	nucleotide binding
D	0000271	biological_process	polysaccharide biosynthetic process
D	0003954	molecular_function	NADH dehydrogenase activity
D	0004617	molecular_function	phosphoglycerate dehydrogenase activity
D	0006065	biological_process	UDP-glucuronate biosynthetic process
D	0009103	biological_process	lipopolysaccharide biosynthetic process
D	0009243	biological_process	O antigen biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0051262	biological_process	protein tetramerization
D	0070403	molecular_function	NAD+ binding
D	0070404	molecular_function	NADH binding
D	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAD A 317

Chain	Residue
A	ALA10
A	SER79
A	PRO80
A	ASN81
A	LEU83
A	HIS84
A	HIS87
A	GLU101
A	LYS102
A	PRO103
A	GLN130
A	GLY11
A	TRP171
A	LYS172
A	ASN184
A	HOH319
A	HOH320
A	HOH333
A	HOH337
A	HOH369
A	HOH372
A	HOH404
A	TYR12
B	GLU55
B	HOH470
C	SER37
C	HOH391
A	ILE13
A	TYR32
A	ASP33
A	ILE34
A	ASN35
A	CYS78

---

site_id	AC2
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAD B 317

Chain	Residue
A	GLU55
A	HOH560
B	ALA10
B	GLY11
B	TYR12
B	ILE13
B	TYR32
B	ASP33
B	ILE34
B	CYS78
B	SER79
B	PRO80
B	ASN81
B	LEU83
B	HIS84
B	HIS87
B	GLU101
B	LYS102
B	PRO103
B	GLN130
B	TRP171
B	LYS172
B	ASN184
B	HIS266
B	HOH334
B	HOH340
B	HOH361
B	HOH365
B	HOH401
B	HOH461
D	SER37
D	HOH348
D	HOH920

---

site_id	AC3
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAD C 317

Chain	Residue
A	SER37
A	HOH446
C	ALA10
C	GLY11
C	TYR12
C	ILE13
C	TYR32
C	ASP33
C	ILE34
C	CYS78
C	SER79
C	PRO80
C	ASN81
C	LEU83
C	HIS84
C	HIS87
C	GLU101
C	LYS102
C	PRO103
C	GLN130
C	TRP171
C	LYS172
C	ASN184
C	HIS266
C	HOH322
C	HOH327
C	HOH342
C	HOH344
C	HOH352
C	HOH353
C	HOH359
C	HOH416
D	GLU55

---

site_id	AC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD D 317

Chain	Residue
B	SER37
B	HOH465
C	GLU55
C	HOH448
D	ALA10
D	GLY11
D	TYR12
D	ILE13
D	TYR32
D	ASP33
D	ILE34
D	ASN35
D	CYS78
D	SER79
D	PRO80
D	ASN81
D	LEU83
D	HIS84
D	HIS87
D	GLU101
D	LYS102
D	GLN130
D	TRP171
D	LYS172
D	ASN184
D	HOH318
D	HOH321
D	HOH329
D	HOH330
D	HOH345
D	HOH616

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20690587","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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