Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1MFZ

Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006970	biological_process	response to osmotic stress
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0036460	biological_process	cellular response to cell envelope stress
A	0042121	biological_process	alginic acid biosynthetic process
A	0044010	biological_process	single-species biofilm formation
A	0047919	molecular_function	GDP-mannose 6-dehydrogenase activity
A	0051287	molecular_function	NAD binding
B	0006970	biological_process	response to osmotic stress
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0036460	biological_process	cellular response to cell envelope stress
B	0042121	biological_process	alginic acid biosynthetic process
B	0044010	biological_process	single-species biofilm formation
B	0047919	molecular_function	GDP-mannose 6-dehydrogenase activity
B	0051287	molecular_function	NAD binding
C	0006970	biological_process	response to osmotic stress
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0036460	biological_process	cellular response to cell envelope stress
C	0042121	biological_process	alginic acid biosynthetic process
C	0044010	biological_process	single-species biofilm formation
C	0047919	molecular_function	GDP-mannose 6-dehydrogenase activity
C	0051287	molecular_function	NAD binding
D	0006970	biological_process	response to osmotic stress
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0036460	biological_process	cellular response to cell envelope stress
D	0042121	biological_process	alginic acid biosynthetic process
D	0044010	biological_process	single-species biofilm formation
D	0047919	molecular_function	GDP-mannose 6-dehydrogenase activity
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GDX D 501

Chain	Residue
C	GLU157
C	ASN225
D	TYR256
D	TYR257
D	MSE258
D	ARG259
D	PHE262
D	PHE264
D	GLY265
D	CYS268
D	LEU269
C	PHE158
D	PHE323
D	LYS324
D	HOH510
C	LEU159
C	ARG160
C	GLU161
C	LYS210
C	ASN214
C	HIS217
C	VAL221

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GDX D 502

Chain	Residue
C	TYR256
C	TYR257
C	MSE258
C	ARG259
C	GLY261
C	PHE262
C	PHE264
C	GLY265
C	CYS268
C	PHE323
C	LYS324
D	TYR10
D	GLU157
D	PHE158
D	LEU159
D	ARG160
D	GLU161
D	LYS210
D	ASN214
D	HIS217
D	VAL221
D	ASN225
D	HOH519

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GDX B 503

Chain	Residue
A	GLU157
A	PHE158
A	LEU159
A	ARG160
A	GLU161
A	LYS210
A	ASN214
A	HIS217
A	VAL221
A	ASN225
B	LEU251
B	TYR256
B	TYR257
B	MSE258
B	ARG259
B	PHE262
B	PHE264
B	GLY265
B	CYS268
B	LEU269
B	PHE323
B	LYS324
B	HOH506
B	HOH507

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GDX B 504

Chain	Residue
A	TYR256
A	TYR257
A	MSE258
A	ARG259
A	GLY261
A	PHE262
A	PHE264
A	GLY265
A	CYS268
A	LEU269
A	PHE323
A	LYS324
B	GLU157
B	PHE158
B	LEU159
B	ARG160
B	GLU161
B	LYS210
B	ASN214
B	HIS217
B	VAL221
B	ASN225

Functional Information from PROSITE/UniProt

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCNVWH

Chain	Residue	Details
A	TYR211-HIS217

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12705829","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"12705829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MV8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"12705829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MUU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"12705829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MUU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"12705829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MV8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1dli

Chain	Residue	Details
A	ASP272
A	CYS268
A	GLU161
A	THR124
A	ASN214
A	LYS210

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1dli

Chain	Residue	Details
B	ASP272
B	CYS268
B	GLU161
B	THR124
B	ASN214
B	LYS210

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1dli

Chain	Residue	Details
C	ASP272
C	CYS268
C	GLU161
C	THR124
C	ASN214
C	LYS210

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1dli

Chain	Residue	Details
D	ASP272
D	CYS268
D	GLU161
D	THR124
D	ASN214
D	LYS210

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)